Peripheral Membrane Proteins最新文献

Folding and Binding Properties of Human Complement Receptor Type 1 Extracellular Domain 人补体受体1型胞外结构域的折叠和结合特性

Peripheral Membrane Proteins Pub Date : 2018-07-25 DOI: 10.5772/INTECHOPEN.75120

N. Ishii

{"title":"Folding and Binding Properties of Human Complement Receptor Type 1 Extracellular Domain","authors":"N. Ishii","doi":"10.5772/INTECHOPEN.75120","DOIUrl":"https://doi.org/10.5772/INTECHOPEN.75120","url":null,"abstract":"Complement receptor type 1 (CR1 or CD35) is a peripheral glycosylated membrane pro- tein that regulates the complement activation in the control of immune responses. The author would like to overview the folding and binding properties of the soluble form of CR1, so-called as sCR1, introducing our development of the high-yield overexpression and purification methods as well as the investigation to its molecular structure. Although sCR1 prepared through our method showed the highest binding affinity against C3b, it is quite difficult to be crystallized for X-ray structure analysis. In spite of many attempts, only microcrystals have been obtained so far. Considering the usefulness to understand factors within the difficulty, the primary sequence of sCR1 has been reexamined from the viewpoints both of secondary structure predictions and recent findings of intrinsi cally disordered proteins (IDPs) or natively unfolded proteins (NUPs). As an example, the theoretically predicted structure of a short consensus repeat (SCR) of a binding domain, SCR-15–17 in sCR1 is compared with the reported solution structure by NMR. The discus - sion is extended to protein structure studies with proteins containing ID regions, which are unfolded state without taking uniformly decided structures.","PeriodicalId":181544,"journal":{"name":"Peripheral Membrane Proteins","volume":"29 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2018-07-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"127560825","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: 0

Rapid Endosomal Recycling 内体快速循环

Peripheral Membrane Proteins Pub Date : 2018-07-25 DOI: 10.5772/INTECHOPEN.75685

Hana Mahmutefendic, Gordana Blagojević Zagorac, S. Macesic, P. Lučin

引用次数: 3

The Function of Fission Yeast Rho1-GEFs in the Control of Cell Growth and Division 裂变酵母Rho1-GEFs对细胞生长和分裂的调控作用

Peripheral Membrane Proteins Pub Date : 2018-07-25 DOI: 10.5772/INTECHOPEN.75913

Tomás Edreira, E. Manjón, Y. Sánchez

{"title":"The Function of Fission Yeast Rho1-GEFs in the Control of Cell Growth and Division","authors":"Tomás Edreira, E. Manjón, Y. Sánchez","doi":"10.5772/INTECHOPEN.75913","DOIUrl":"https://doi.org/10.5772/INTECHOPEN.75913","url":null,"abstract":"Guanine nucleotide exchange factors (GEFs) are directly responsible for the activation of Rho-family GTPases in response to physical and chemical stimuli and ultimately regulate numerous cellular responses such as polarized growth, morphogenesis, and movement. The GEF proteins are characterized by a Dbl-homology (DH) domain that contacts the Rho GTPases, to catalyzing nucleotide exchange, and an associated Pleckstrin homology (PH) domain, which fine-tunes the exchange process by a variety of mechanisms related to the binding of phosphoinositides. Most GEFs are divergent in regions outside the DH/ PH module and contain additional protein-protein or lipid-protein interaction domains that presumably dictate unique cellular functions. Fission yeast Rho1-GEFs act as a link between growth processes and the cell cycle machinery. In this chapter, we focus on the recent leaps in our understanding of how Rho1-GEFs control interphase and cytokinesis in fission yeast. Furthermore, we will go beyond mitosis and highlight the unexpected roles of Rho1-GEFs in the DNA damage response. in cell division. Double-mutant and phenotypic complementation results suggest that Rgf1p and Rgf3p are not functionally exchangeable. Disruption of rgf1 + in an rgf3 mutant ( ehs2-1 ) produced viable cells at 28°C but not at 37°C,","PeriodicalId":181544,"journal":{"name":"Peripheral Membrane Proteins","volume":"323 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2018-07-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"122334200","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: 0

The Function of Rab35 in Development and Disease Rab35在发育和疾病中的作用

Peripheral Membrane Proteins Pub Date : 2018-07-25 DOI: 10.5772/INTECHOPEN.75168

Jia L. Song, M. Testa

引用次数: 2

Introductory Chapter: Invitation for Peripheral Membrane Proteins 导论:外周膜蛋白的邀约

Peripheral Membrane Proteins Pub Date : 2018-07-25 DOI: 10.5772/INTECHOPEN.79512

Shihori Tanabe

引用次数: 0

Biosensing Techniques in Yeast: G-Protein Signaling and Protein-Protein Interaction Assays for Monitoring Ligand Stimulation and Oligomer Formation of Heterologous GPCRs 酵母的生物传感技术:g蛋白信号和蛋白相互作用检测用于监测配体刺激和异源gpcr的低聚物形成

Peripheral Membrane Proteins Pub Date : 2018-07-25 DOI: 10.5772/INTECHOPEN.76330

Yasuyuki Nakamura, A. Kondo, Jun Ishii

引用次数: 1

Aberrant SGK1 Transcription in LNCaP: A Novel Feed-back Mechanism of TGF-beta1 Regulation in Prostate Carcinogenesis LNCaP中SGK1的异常转录:tgf - β 1调控前列腺癌发生的一种新的反馈机制

Peripheral Membrane Proteins Pub Date : 2018-03-15 DOI: 10.5772/INTECHOPEN.75165

X. Leighton, H. Pollard, M. Srivastava

引用次数: 0