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Annual review of biophysics and biomolecular structure最新文献

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Structure and function of natural killer cell surface receptors. 自然杀伤细胞表面受体的结构与功能。
Annual review of biophysics and biomolecular structure Pub Date : 2003-01-01 Epub Date: 2002-12-02 DOI: 10.1146/annurev.biophys.32.110601.142347
Sergei Radaev, Peter D Sun
{"title":"Structure and function of natural killer cell surface receptors.","authors":"Sergei Radaev,&nbsp;Peter D Sun","doi":"10.1146/annurev.biophys.32.110601.142347","DOIUrl":"https://doi.org/10.1146/annurev.biophys.32.110601.142347","url":null,"abstract":"<p><p>Since mid-1990, with cloning and identification of several families of natural killer (NK) receptors, research on NK cells began to receive appreciable attention. Determination of structures of NK cell surface receptors and their ligand complexes led to a fast growth in our understanding of the activation and ligand recognition by these receptors as well as their function in innate immunity. Functionally, NK cell surface receptors are divided into two groups, the inhibitory and the activating receptors. Structurally, they belong to either the immunoglobulin (Ig)-like receptor superfamily or the C-type lectin-like receptor (CTLR) superfamily. Their ligands are either members of class I major histocompatibility complexes (MHC) or homologs of class I MHC molecules. The inhibitory form of NK receptors provides the protective immunity through recognizing class I MHC molecules with self-peptides on healthy host cells. The activating, or the noninhibitory, NK receptors mediate the killing of tumor or virally infected cells through their specific ligand recognition. The structures of activating and inhibitory NK cell surface receptors and their complexes with the ligands determined to date, including killer immunoglobulin-like receptors (KIRs) and their complexes with HLA molecules, CD94, Ly49A, and its complex with H-2Dd, and NKG2D receptors and their complexes with class I MHC homologs, are reviewed here.</p>","PeriodicalId":8270,"journal":{"name":"Annual review of biophysics and biomolecular structure","volume":"32 ","pages":"93-114"},"PeriodicalIF":0.0,"publicationDate":"2003-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.biophys.32.110601.142347","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"22144598","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 95
The state of lipid rafts: from model membranes to cells. 脂筏的状态:从模型膜到细胞。
Annual review of biophysics and biomolecular structure Pub Date : 2003-01-01 Epub Date: 2003-01-16 DOI: 10.1146/annurev.biophys.32.110601.142439
Michael Edidin
{"title":"The state of lipid rafts: from model membranes to cells.","authors":"Michael Edidin","doi":"10.1146/annurev.biophys.32.110601.142439","DOIUrl":"https://doi.org/10.1146/annurev.biophys.32.110601.142439","url":null,"abstract":"<p><p>Lipid raft microdomains were conceived as part of a mechanism for the intracellular trafficking of lipids and lipid-anchored proteins. The raft hypothesis is based on the behavior of defined lipid mixtures in liposomes and other model membranes. Experiments in these well-characterized systems led to operational definitions for lipid rafts in cell membranes. These definitions, detergent solubility to define components of rafts, and sensitivity to cholesterol deprivation to define raft functions implicated sphingolipid- and cholesterol-rich lipid rafts in many cell functions. Despite extensive work, the basis for raft formation in cell membranes and the size of rafts and their stability are all uncertain. Recent work converges on very small rafts <10 nm in diameter that may enlarge and stabilize when their constituents are cross-linked.</p>","PeriodicalId":8270,"journal":{"name":"Annual review of biophysics and biomolecular structure","volume":"32 ","pages":"257-83"},"PeriodicalIF":0.0,"publicationDate":"2003-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.biophys.32.110601.142439","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"22209767","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 1288
Structure and function of the calcium pump. 钙泵的结构和功能。
Annual review of biophysics and biomolecular structure Pub Date : 2003-01-01 Epub Date: 2003-02-19 DOI: 10.1146/annurev.biophys.32.110601.142433
David L Stokes, N Michael Green
{"title":"Structure and function of the calcium pump.","authors":"David L Stokes,&nbsp;N Michael Green","doi":"10.1146/annurev.biophys.32.110601.142433","DOIUrl":"https://doi.org/10.1146/annurev.biophys.32.110601.142433","url":null,"abstract":"<p><p>Active transport of cations is achieved by a large family of ATP-dependent ion pumps, known as P-type ATPases. Various members of this family have been targets of structural and functional investigations for over four decades. Recently, atomic structures have been determined for Ca2+-ATPase by X-ray crystallography, which not only reveal the architecture of these molecules but also offer the opportunity to understand the structural mechanisms by which the energy of ATP is coupled to calcium transport across the membrane. This energy coupling is accomplished by large-scale conformational changes. The transmembrane domain undergoes plastic deformations under the influence of calcium binding at the transport site. Cytoplasmic domains undergo dramatic rigid-body movements that deliver substrates to the catalytic site and that establish new domain interfaces. By comparing various structures and correlating functional data, we can now begin to associate the chemical changes constituting the reaction cycle with structural changes in these domains.</p>","PeriodicalId":8270,"journal":{"name":"Annual review of biophysics and biomolecular structure","volume":"32 ","pages":"445-68"},"PeriodicalIF":0.0,"publicationDate":"2003-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.biophys.32.110601.142433","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"22256653","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 87
Acetylcholine binding protein (AChBP): a secreted glial protein that provides a high-resolution model for the extracellular domain of pentameric ligand-gated ion channels. 乙酰胆碱结合蛋白(Acetylcholine binding protein, AChBP):一种分泌性胶质蛋白，为五聚体配体门控离子通道的胞外结构域提供了高分辨率模型。
Annual review of biophysics and biomolecular structure Pub Date : 2003-01-01 Epub Date: 2003-02-21 DOI: 10.1146/annurev.biophys.32.110601.142536
Titia K Sixma, August B Smit
{"title":"Acetylcholine binding protein (AChBP): a secreted glial protein that provides a high-resolution model for the extracellular domain of pentameric ligand-gated ion channels.","authors":"Titia K Sixma,&nbsp;August B Smit","doi":"10.1146/annurev.biophys.32.110601.142536","DOIUrl":"https://doi.org/10.1146/annurev.biophys.32.110601.142536","url":null,"abstract":"<p><p>Acetylcholine binding protein (AChBP) has recently been identified from molluskan glial cells. Glial cells secrete it into cholinergic synapses, where it plays a role in modulating synaptic transmission. This novel mechanism resembles glia-dependent modulation of glutamate synapses, with several key differences. AChBP is a homolog of the ligand binding domain of the pentameric ligand-gated ion-channels. The crystal structure of AChBP provides the first high-resolution structure for this family of Cys-loop receptors. Nicotinic acetylcholine receptors and related ion-channels such as GABAA, serotonin 5HT3, and glycine can be interpreted in the light of the 2.7 A AChBP structure. The structural template provides critical details of the binding site and helps create models for toxin binding, mutational effects, and molecular gating.</p>","PeriodicalId":8270,"journal":{"name":"Annual review of biophysics and biomolecular structure","volume":"32 ","pages":"311-34"},"PeriodicalIF":0.0,"publicationDate":"2003-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.biophys.32.110601.142536","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"22341442","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 144
Molecular recognition and docking algorithms. 分子识别和对接算法。
Annual review of biophysics and biomolecular structure Pub Date : 2003-01-01 Epub Date: 2003-01-28 DOI: 10.1146/annurev.biophys.32.110601.142532
Natasja Brooijmans, Irwin D Kuntz
{"title":"Molecular recognition and docking algorithms.","authors":"Natasja Brooijmans,&nbsp;Irwin D Kuntz","doi":"10.1146/annurev.biophys.32.110601.142532","DOIUrl":"https://doi.org/10.1146/annurev.biophys.32.110601.142532","url":null,"abstract":"<p><p>Molecular docking is an invaluable tool in modern drug discovery. This review focuses on methodological developments relevant to the field of molecular docking. The forces important in molecular recognition are reviewed and followed by a discussion of how different scoring functions account for these forces. More recent applications of computational chemistry tools involve library design and database screening. Last, we summarize several critical methodological issues that must be addressed in future developments.</p>","PeriodicalId":8270,"journal":{"name":"Annual review of biophysics and biomolecular structure","volume":"32 ","pages":"335-73"},"PeriodicalIF":0.0,"publicationDate":"2003-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.biophys.32.110601.142532","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"22234814","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 677
The power and prospects of fluorescence microscopies and spectroscopies. 荧光显微镜和光谱学的力量和前景。
Annual review of biophysics and biomolecular structure Pub Date : 2003-01-01 Epub Date: 2003-02-11 DOI: 10.1146/annurev.biophys.32.110601.142525
Xavier Michalet, Achillefs N Kapanidis, Ted Laurence, Fabien Pinaud, Soeren Doose, Malte Pflughoefft, Shimon Weiss
{"title":"The power and prospects of fluorescence microscopies and spectroscopies.","authors":"Xavier Michalet,&nbsp;Achillefs N Kapanidis,&nbsp;Ted Laurence,&nbsp;Fabien Pinaud,&nbsp;Soeren Doose,&nbsp;Malte Pflughoefft,&nbsp;Shimon Weiss","doi":"10.1146/annurev.biophys.32.110601.142525","DOIUrl":"https://doi.org/10.1146/annurev.biophys.32.110601.142525","url":null,"abstract":"<p><p>Recent years have witnessed a renaissance of fluorescence microscopy techniques and applications, from live-animal multiphoton confocal microscopy to single-molecule fluorescence spectroscopy and imaging in living cells. These achievements have been made possible not so much because of improvements in microscope design, but rather because of development of new detectors, accessible continuous wave and pulsed laser sources, sophisticated multiparameter analysis on one hand, and the development of new probes and labeling chemistries on the other. This review tracks the lineage of ideas and the evolution of thinking that have led to the actual developments, and presents a comprehensive overview of the field, with emphasis put on our laboratory's interest in single-molecule microscopy and spectroscopy.</p>","PeriodicalId":8270,"journal":{"name":"Annual review of biophysics and biomolecular structure","volume":"32 ","pages":"161-82"},"PeriodicalIF":0.0,"publicationDate":"2003-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.biophys.32.110601.142525","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"22256656","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 213
Single-particle imaging of macromolecules by cryo-electron microscopy. 低温电子显微镜下大分子的单粒子成像。
Annual review of biophysics and biomolecular structure Pub Date : 2002-01-01 DOI: 10.1146/ANNUREV.BIOPHYS.31.082901.134202
J. Frank
{"title":"Single-particle imaging of macromolecules by cryo-electron microscopy.","authors":"J. Frank","doi":"10.1146/ANNUREV.BIOPHYS.31.082901.134202","DOIUrl":"https://doi.org/10.1146/ANNUREV.BIOPHYS.31.082901.134202","url":null,"abstract":"Cryo-electron microscopy (cryo-EM) of biological molecules in single-particle (i.e., unordered, nonaggregated) form is a new approach to the study of molecular assemblies, which are often too large and flexible to be amenable to X-ray crystallography. New insights into biological function on the molecular level are expected from cryo-EM applied to the study of such complexes \"trapped\" at different stages of their conformational changes and dynamical interactions. Important molecular machines involved in the fundamental processes of transcription, mRNA splicing, and translation are examples for successful applications of the new technique, combined with structural knowledge gained by conventional techniques of structure determination, such as X-ray crystallography and NMR.","PeriodicalId":8270,"journal":{"name":"Annual review of biophysics and biomolecular structure","volume":"38 1","pages":"303-19"},"PeriodicalIF":0.0,"publicationDate":"2002-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81460951","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 350
NMR studies of lipoprotein structure. 脂蛋白结构的核磁共振研究。
Annual review of biophysics and biomolecular structure Pub Date : 2002-01-01 DOI: 10.1146/ANNUREV.BIOPHYS.31.101101.140910
R. J. Cushley, M. Okon
{"title":"NMR studies of lipoprotein structure.","authors":"R. J. Cushley, M. Okon","doi":"10.1146/ANNUREV.BIOPHYS.31.101101.140910","DOIUrl":"https://doi.org/10.1146/ANNUREV.BIOPHYS.31.101101.140910","url":null,"abstract":"Early NMR structural studies of serum lipoproteins were based on (1)H, (13)C, (31)P, and (2)H studies of lipid components. From the early studies information on composition, lipid chain dynamics and order parameters, and monolayer organization resulted. More recently, selective or complete isotopic labeling techniques, combined with multidimensional NMR spectroscopy, have resulted in structural information of apoprotein fragments. Finally, use of heteronuclear three- and four-dimensional experiments have yielded solution structures and protein-lipid interactions of intact apolipoproteins C-I, C-II, and A-I.","PeriodicalId":8270,"journal":{"name":"Annual review of biophysics and biomolecular structure","volume":"59 1","pages":"177-206"},"PeriodicalIF":0.0,"publicationDate":"2002-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"80105520","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 40
PIP(2) and proteins: interactions, organization, and information flow. PIP(2)与蛋白质:相互作用、组织和信息流。
Annual review of biophysics and biomolecular structure Pub Date : 2002-01-01 DOI: 10.1146/ANNUREV.BIOPHYS.31.082901.134259
S. McLaughlin, Jiyao Wang, A. Gambhir, D. Murray
{"title":"PIP(2) and proteins: interactions, organization, and information flow.","authors":"S. McLaughlin, Jiyao Wang, A. Gambhir, D. Murray","doi":"10.1146/ANNUREV.BIOPHYS.31.082901.134259","DOIUrl":"https://doi.org/10.1146/ANNUREV.BIOPHYS.31.082901.134259","url":null,"abstract":"We review the physical properties of phosphatidylinositol 4,5-bisphosphate (PIP2) that determine both its specific interactions with protein domains of known structure and its nonspecific electrostatic sequestration by unstructured domains. Several investigators have postulated the existence of distinct pools of PIP2 within the cell to account for the myriad functions of this lipid. Recent experimental work indicates certain regions of the plasma membrane-membrane ruffles and nascent phagosomes-do indeed concentrate PIP2. We consider two mechanisms that could account for this phenomenon: local synthesis and electrostatic sequestration. We conclude by considering the hypothesis that proteins such as MARCKS bind a significant fraction of the PIP2 in a cell, helping to sequester it in lateral membrane domains, then release this lipid in response to local signals such as an increased concentration of Ca(++)/calmodulin or activation of protein kinase C.","PeriodicalId":8270,"journal":{"name":"Annual review of biophysics and biomolecular structure","volume":"110 1","pages":"151-75"},"PeriodicalIF":0.0,"publicationDate":"2002-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87654081","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 752
Paramagnetic resonance of biological metal centers. 生物金属中心的顺磁共振。
Annual review of biophysics and biomolecular structure Pub Date : 2002-01-01 DOI: 10.1146/ANNUREV.BIOPHYS.31.091701.171000
M. Ubbink, J. Worrall, G. Canters, E. Groenen, Martina Huber
{"title":"Paramagnetic resonance of biological metal centers.","authors":"M. Ubbink, J. Worrall, G. Canters, E. Groenen, Martina Huber","doi":"10.1146/ANNUREV.BIOPHYS.31.091701.171000","DOIUrl":"https://doi.org/10.1146/ANNUREV.BIOPHYS.31.091701.171000","url":null,"abstract":"The review deals with recent advances in magnetic resonance spectroscopy (hf EPR and NMR) of paramagnetic metal centers in biological macromolecules. In the first half of our chapter, we present an overview of recent technical developments in the NMR of paramagnetic bio-macromolecules. These are illustrated by a variety of examples deriving mainly from the spectroscopy of metalloproteins and their complexes. The second half focuses on recent developments in high-frequency EPR spectroscopy and the application of the technique to copper, iron, and manganese proteins. Special attention is given to the work on single crystals of copper proteins.","PeriodicalId":8270,"journal":{"name":"Annual review of biophysics and biomolecular structure","volume":"73 1","pages":"393-422"},"PeriodicalIF":0.0,"publicationDate":"2002-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89258768","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 101
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