Unmasking the annexin I interaction from the structure of apo-S100A11
Unmasking the annexin I interaction from the structure of apo-S100A11
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DOI：
10.1016/s0969-2126(03)00126-6
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发表时间：
2003-07-01
期刊：
影响因子：
5.7
通讯作者：
Shaw, GS
中科院分区：
文献类型：
--
作者：
Dempsey, AC;Walsh, MP;Shaw, GS
S100A11 是一种同二聚体 EF-hand 钙结合蛋白，经历钙诱导的构象变化并与磷脂结合蛋白膜联蛋白 I 相互作用以协调膜结合。在这项工作中，通过核磁共振波谱确定了 apo-S100A11 的溶液结构，以揭示其钙诱导的结构变化的细节。 Apo-S100A11 形成紧密的球状结构，在钙结合位点 II 中具有接近反平行方向的螺旋 III 和 IV。此外，螺旋 I 和 IV、以及 I 和 I' 形成比在其他 apo-S100 蛋白中观察到的更紧密的排列。 apo-S100A11 中的这种螺旋排列将残基部分埋入螺旋 I (P3、E11、A15)、III (V55、R58、M59) 和 IV (A86、C87、S90) 以及接头 (A45、F46) 中，这是在钙结合状态下与膜联蛋白 I 相互作用所必需的。在 apo-S100A11 中，这会产生“掩蔽”的结合表面，该表面阻止膜联蛋白 I 结合，但在钙结合时被暴露。
S100A11 is a homodimeric EF-hand calcium binding protein that undergoes a calcium-induced conformational change and interacts with the phospholipid binding protein annexin I to coordinate membrane association. In this work, the solution structure of apo-S100A11 has been determined by NMR spectroscopy to uncover the details of its calcium-induced structural change. Apo-S100A11 forms a tight globular structure having a near antiparallel orientation of helices III and IV in calcium binding site II. Further, helices I and IV, and I and I', form a more closed arrangement than observed in other apo-S100 proteins. This helix arrangement in apo-S100A11 partially buries residues in helices I (P3, E11, A15), III (V55, R58, M59), and IV (A86, C87, S90) and the linker (A45, F46), which are required for interaction with annexin I in the calcium-bound state. In apo-S100A11, this results in a "masked" binding surface that prevents annexin I binding but is uncovered upon calcium binding.