Structural basis of collagen recognition by integrin α2β1
Structural basis of collagen recognition by integrin α2β1
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DOI：
10.1016/s0092-8674(00)80622-4
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发表时间：
2000-03-31
期刊：
影响因子：
64.5
通讯作者：
Liddington, RC
中科院分区：
文献类型：
--
作者：
Emsley, J;Knight, CG;Liddington, RC
我们已经确定了整合素α2β1的I结构域与含有关键的GFOGER基序的三螺旋胶原蛋白肽之间的复合物的晶体结构。I结构域上表面协调金属离子的三个环也与胶原蛋白结合，胶原蛋白的谷氨酸完成了金属的配位球。与未结合配体的I结构域相比，揭示了金属配位的变化与上表面的重组相关联，这两者共同为结合胶原蛋白创造了一个互补的表面。构象变化从I结构域的上表面传播到其相对的极点，这提示了亲和力调节的基础以及信号转导的途径。此处观察到的结构特征可能代表了整合素 - 配体识别的一种通用机制。
We have determined the crystal structure of a complex between the I domain of integrin alpha 2 beta 1 and a triple helical collagen peptide containing a critical GFOGER motif. Three loops on the upper surface of the I domain that coordinate a metal ion also engage the collagen, with a collagen glutamate completing the coordination sphere of the metal. Comparison with the unliganded I domain reveals a change in metal coordination linked to a reorganization of the upper surface that together create a complementary surface for binding collagen. Conformational changes propagate from the upper surface to the opposite pole of the domain, suggesting both a basis for affinity regulation and a pathway for signal transduction. The structural features observed here may represent a general mechanism for integrin-ligand recognition.