THE 3-DIMENSIONAL STRUCTURE OF THE 10TH TYPE-III MODULE OF FIBRONECTIN - AN INSIGHT INTO RGD-MEDIATED INTERACTIONS
THE 3-DIMENSIONAL STRUCTURE OF THE 10TH TYPE-III MODULE OF FIBRONECTIN - AN INSIGHT INTO RGD-MEDIATED INTERACTIONS
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DOI：
10.1016/0092-8674(92)90600-h
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发表时间：
1992-11-13
期刊：
影响因子：
64.5
通讯作者：
CAMPBELL, ID
中科院分区：
文献类型：
--
作者：
MAIN, AL;HARVEY, TS;CAMPBELL, ID
已确定使用核磁共振技术的纤连蛋白的第十个III型模块的解决方案的结构。该分子具有与免疫球蛋白结构域相似的折叠，其中七条β链形成两个反平行的β折叠，它们相互挤压。两种β折叠都将保守的疏水残基贡献给紧凑的核心。与免疫球蛋白C结构域相比，其拓扑结构更类似于CD 4、PapD的结构域2和人生长激素受体的细胞外结构域。该模块包含已知参与细胞粘附的Arg-Gly-Asp序列。该三肽是溶剂暴露的，位于链F和G之间的构象移动的环上，与其细胞粘附功能一致。
The solution structure of the tenth type III module of fibronectin has been determined using nuclear magnetic resonance techniques. The molecule has a fold similar to that of immunoglobulin domains, with seven beta strands forming two antiparallel beta sheets, which pack against each other. Both beta sheets contribute conserved hydrophobic residues to a compact core. The topology is more similar to that of domain 2 of CD4, PapD, and the extracellular domain of the human growth hormone receptor than to that of immunoglobulin C domains. The module contains an Arg-Gly-Asp sequence known to be involved in cell adhesion. This tripeptide is solvent exposed and lies on a conformationally mobile loop between strands F and G, consistent with its cell adhesion function.