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血小板受体与纤维状胶原蛋白相互作用的结构见解

Structural insights into the interactions between platelet receptors and fibrillar collagen.

作者信息

Herr Andrew B, Farndale Richard W

机构信息

Department of Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati College of Medicine, Cincinnati, Ohio 45267-0524, USA.

出版信息

J Biol Chem. 2009 Jul 24;284(30):19781-5. doi: 10.1074/jbc.R109.013219. Epub 2009 Apr 28.

DOI:10.1074/jbc.R109.013219
PMID:19401461
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2740402/
Abstract

Collagen peptides have been used to identify binding sites for several important collagen receptors, including integrin alpha(2)beta(1), glycoprotein VI, and von Willebrand factor. In parallel, the structures of these collagen receptors have been reported, and their interactions with collagen peptides have been studied. Recently, the three-dimensional structure of the intact type I collagen fiber from rat tail tendon has been resolved by fiber diffraction. It is now possible to map the binding sites of platelet collagen receptors onto the intact collagen fiber in three dimensions. This minireview will discuss these recent findings and their implications for platelet activation by collagen.

摘要

胶原蛋白肽已被用于识别几种重要的胶原蛋白受体的结合位点,包括整合素α(2)β(1)、糖蛋白VI和血管性血友病因子。与此同时,这些胶原蛋白受体的结构也已被报道,并且它们与胶原蛋白肽的相互作用也已得到研究。最近,通过纤维衍射解析了来自大鼠尾腱的完整I型胶原纤维的三维结构。现在有可能在三维空间中将血小板胶原蛋白受体的结合位点映射到完整的胶原纤维上。这篇综述将讨论这些最新发现及其对胶原蛋白诱导血小板激活的意义。

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本文引用的文献

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Identification and structural analysis of type I collagen sites in complex with fibronectin fragments.与纤连蛋白片段复合的I型胶原蛋白位点的鉴定与结构分析。
Proc Natl Acad Sci U S A. 2009 Mar 17;106(11):4195-200. doi: 10.1073/pnas.0812516106. Epub 2009 Feb 27.
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Structural basis of sequence-specific collagen recognition by SPARC.SPARC对序列特异性胶原蛋白识别的结构基础。
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Identification of FcgammaRIIa as the ITAM-bearing receptor mediating alphaIIbbeta3 outside-in integrin signaling in human platelets.鉴定FcγRIIa为在人血小板中介导αIIbβ3外向整合素信号传导的含免疫受体酪氨酸激活基序的受体。
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Biochem Soc Trans. 2008 Apr;36(Pt 2):241-50. doi: 10.1042/BST0360241.
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Identification of a major GpVI-binding locus in human type III collagen.人类III型胶原蛋白中一个主要的糖蛋白VI结合位点的鉴定。
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Collagen fibril architecture, domain organization, and triple-helical conformation govern its proteolysis.胶原纤维结构、结构域组织和三螺旋构象决定其蛋白水解过程。
Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):2824-9. doi: 10.1073/pnas.0710588105. Epub 2008 Feb 14.
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Characterization of high affinity binding motifs for the discoidin domain receptor DDR2 in collagen.胶原蛋白中盘状结构域受体DDR2的高亲和力结合基序的表征
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Ligand binding rapidly induces disulfide-dependent dimerization of glycoprotein VI on the platelet plasma membrane.配体结合迅速诱导血小板质膜上糖蛋白VI的二硫键依赖性二聚化。
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