Advances in Protein Chemistry最新文献_第2页

Beta-rolls, beta-helices, and other beta-solenoid proteins. -卷，-螺旋和其他-螺线管蛋白。

Advances in Protein Chemistry Pub Date : 2006-01-01 DOI: 10.1016/S0065-3233(06)73003-0

Andrey V Kajava, Alasdair C Steven

{"title":"Beta-rolls, beta-helices, and other beta-solenoid proteins.","authors":"Andrey V Kajava, Alasdair C Steven","doi":"10.1016/S0065-3233(06)73003-0","DOIUrl":"https://doi.org/10.1016/S0065-3233(06)73003-0","url":null,"abstract":"Beta-rolls and beta-helices belong to a larger group of topologically similar proteins with solenoid folds: because their regular secondary structure elements are exclusively beta-strands, they are referred to as beta-solenoids. The number of beta-solenoids whose structures are known is now large enough to support a systematic analysis. Here we survey the distinguishing structural features of beta-solenoids, also documenting their notable diversity. Appraisal of these structures suggests a classification based on handedness, twist, oligomerization state, and coil shape. In addition, beta-solenoids are distinguished by the number of chains that wind around a common axis: the majority are single-stranded but there is a recently discovered subset of triple-stranded beta-solenoids. This survey has revealed some relationships of the amino acid sequences of beta-solenoids with their structures and functions-in particular, the repetitive character of the coil sequences and conformations that recur in tracts of tandem repeats. We have proposed the term beta-arc for the distinctive turns found in beta-solenoids and beta-arch for the corresponding strand-turn-strand motifs. The evolutionary mechanisms underlying these proteins are also discussed. This analysis has direct implications for sequence-based detection, structural prediction, and de novo design of other beta-solenoid proteins. The abundance of virulence factors, toxins and allergens among beta-solenoids, as well as commonalities of beta-solenoids with amyloid fibrils, imply that this class of folds may have a broader role in human diseases than was previously recognized. Thus, identification of genes with putative beta-solenoid domains promises to be a fertile direction in the search for viable targets in the development of new antibiotics and vaccines.","PeriodicalId":51216,"journal":{"name":"Advances in Protein Chemistry","volume":"73 ","pages":"55-96"},"PeriodicalIF":0.0,"publicationDate":"2006-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0065-3233(06)73003-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26461782","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: 106

From the polymorphism of amyloid fibrils to their assembly mechanism and cytotoxicity. 从淀粉样原纤维的多态性到其组装机制和细胞毒性。

Advances in Protein Chemistry Pub Date : 2006-01-01 DOI: 10.1016/S0065-3233(06)73007-8

Laurent Kreplak, Ueli Aebi

引用次数: 45

Structural models of amyloid-like fibrils. 淀粉样原纤维的结构模型。

Advances in Protein Chemistry Pub Date : 2006-01-01 DOI: 10.1016/S0065-3233(06)73008-X

Rebecca Nelson, David Eisenberg

{"title":"Structural models of amyloid-like fibrils.","authors":"Rebecca Nelson, David Eisenberg","doi":"10.1016/S0065-3233(06)73008-X","DOIUrl":"https://doi.org/10.1016/S0065-3233(06)73008-X","url":null,"abstract":"Amyloid fibrils are elongated, insoluble protein aggregates deposited in vivo in amyloid diseases, and amyloid-like fibrils are formed in vitro from soluble proteins. Both of these groups of fibrils, despite differences in the sequence and native structure of their component proteins, share common properties, including their core structure. Multiple models have been proposed for the common core structure, but in most cases, atomic-level structural details have yet to be determined. Here we review several structural models proposed for amyloid and amyloid-like fibrils and relate features of these models to the common fibril properties. We divide models into three classes: Refolding, Gain-of-Interaction, and Natively Disordered. The Refolding models propose structurally distinct native and fibrillar states and suggest that backbone interactions drive fibril formation. In contrast, the Gain-of-Interaction models propose a largely native-like structure for the protein in the fibril and highlight the importance of specific sequences in fibril formation. The Natively Disordered models have aspects in common with both Refolding and Gain-of-Interaction models. While each class of model suggests explanations for some of the common fibril properties, and some models, such as Gain-of-Interaction models with a cross-beta spine, fit a wider range of properties than others, no one class provides a complete explanation for all amyloid fibril behavior.","PeriodicalId":51216,"journal":{"name":"Advances in Protein Chemistry","volume":"73 ","pages":"235-82"},"PeriodicalIF":0.0,"publicationDate":"2006-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0065-3233(06)73008-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26519688","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: 192

X-Ray fiber and powder diffraction of PrP prion peptides. PrP朊病毒肽的x射线纤维和粉末衍射。

Advances in Protein Chemistry Pub Date : 2006-01-01 DOI: 10.1016/S0065-3233(06)73006-6

Hideyo Inouye, Daniel A Kirschner

引用次数: 16

Microtubules and maps. 微管和地图。

Advances in Protein Chemistry Pub Date : 2005-01-01 DOI: 10.1016/S0065-3233(04)71007-4

Linda A Amos, Daniel Schlieper

引用次数: 196

How hydrogen bonds shape membrane protein structure. 氢键如何塑造膜蛋白结构。

Advances in Protein Chemistry Pub Date : 2005-01-01 DOI: 10.1016/S0065-3233(05)72006-4

Stephen H White

引用次数: 36

Intermediate filament associated proteins. 中间丝相关蛋白。

Advances in Protein Chemistry Pub Date : 2005-01-01 DOI: 10.1016/S0065-3233(05)70006-1

Kathleen J Green, Michael Böhringer, Todd Gocken, Jonathan C R Jones

引用次数: 6

Structural and functional implications of sequence repeats in fibrous proteins. 纤维蛋白序列重复序列的结构和功能意义。

Advances in Protein Chemistry Pub Date : 2005-01-01 DOI: 10.1016/S0065-3233(05)70002-4

David A D Parry

{"title":"Structural and functional implications of sequence repeats in fibrous proteins.","authors":"David A D Parry","doi":"10.1016/S0065-3233(05)70002-4","DOIUrl":"https://doi.org/10.1016/S0065-3233(05)70002-4","url":null,"abstract":"The amino acid sequences of increasingly large proteins have been determined in recent years, and it has become more and more apparent that within these sequences nature has employed only a finite number of structural?functional motifs. These may be strung along the sequence in tandem and, in some cases, several hundred times. In other instances, the positions of the motifs show little obvious order as regards to their relative linear arrangement within the sequence. The observed sequence repeats have been shown to vary in size over at least two orders of magnitude. It is shown here that the repeats can readily be classified on the basis of character, and five distinct groups have been identified. The first of these (Type A) represents those motifs that are fixed in length and conserved absolutely in sequence (>99%); the second (Type B) includes motifs that are also fixed in length, but where absolute sequence conservation occurs only in some positions of the repeat. The third category (Type C) contains fixed length motifs, but the character of only some of the positions in the motif is maintained. The fourth group (Type D) includes motifs that have nonintegral lengths. The fifth class (Type E) contains motifs, often displaying some variations in their lengths even within a single species, which maintain a discrete structural form related directly to their function. Examples are presented for each category of repeat, and these are drawn almost exclusively from the fibrous proteins and those proteins that are normally associated with them in vivo.","PeriodicalId":51216,"journal":{"name":"Advances in Protein Chemistry","volume":"70 ","pages":"11-35"},"PeriodicalIF":0.0,"publicationDate":"2005-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0065-3233(05)70002-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25063920","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: 15

The structure of alpha-helical coiled coils. 螺旋线圈的结构。

Advances in Protein Chemistry Pub Date : 2005-01-01 DOI: 10.1016/S0065-3233(05)70003-6

Andrei N Lupas, Markus Gruber

引用次数: 561

The molecular mechanism of muscle contraction. 肌肉收缩的分子机制。

Advances in Protein Chemistry Pub Date : 2005-01-01 DOI: 10.1016/S0065-3233(04)71005-0

Michael A Geeves, Kenneth C Holmes

引用次数: 361