Leahy D J, Aukhil I, Erickson H P
Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21218, USA.
Cell. 1996 Jan 12;84(1):155-64. doi: 10.1016/s0092-8674(00)81002-8.
We have determined the 2.0 A crystal structure of a fragment of human fibronectin encompassing the seventh through the RGD-containing tenth type III repeats (FN7-10). The structure reveals an extended rod-like molecule with a long axis of approximately 140 A and highly variable relationships between adjacent domains. An unusually small rotation between domains 9 and 10 creates a distinctive binding site, in which the RGD loop from domain 10 and the "synergy" region from domain 9 are on the same face of FN7-10 and thus easily accessible to a single integrin molecule. The cell-binding RGD loop is well-ordered in this structure and extends approximately 10 A away from the FN7-10 core.
我们已经确定了人纤连蛋白片段的2.0埃晶体结构，该片段包含从第七个到含RGD的第十个III型重复序列（FN7-10）。该结构揭示了一个细长的棒状分子，其长轴约为140埃，相邻结构域之间的关系高度可变。结构域9和10之间异常小的旋转产生了一个独特的结合位点，其中结构域10的RGD环和结构域9的“协同”区域位于FN7-10的同一面上，因此单个整合素分子很容易接近。在该结构中，细胞结合RGD环排列有序，从FN7-10核心向外延伸约10埃。
