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首页> 外文期刊>Journal of Molecular Biology >Crystal structure of EMS16 in complex with the integrin alpha2-I domain.
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Crystal structure of EMS16 in complex with the integrin alpha2-I domain.

机译：具有整联蛋白α2-I结构域的EMS16的晶体结构。

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摘要

Snake venoms contain a number of heterodimeric C-type lectin-like proteins (CLPs) that interact specifically with components of the haemostatic system. EMS16 from the venom of Echis multisquamatus binds to the collagen receptor, integrin alpha2beta1, also known as glycoprotein (GP) Ia/IIa, and specifically inhibits collagen binding. Here we report the crystal structure of EMS16 in complex with recombinant integrin alpha2-I domain that plays a central role in collagen binding. The structure of the complex at 1.9 Angstrom resolution reveals that the collagen-binding site of the alpha2-I domain is covered completely by the bound EMS16. This blockage by EMS16 appears to spatially inhibit collagen binding to the alpha2-I domain. The bound alpha2-I domain adopts a closed conformation, which is seen in the absence of ligand, suggesting that EMS16 stabilizes a closed conformation corresponding to the less active structure of the alpha2-I domain. EMS16 does not directly bind to the manganese ion and residues ofthe metal ion-dependent adhesion site (MIDAS) of the alpha2-I domain, suggesting that EMS16 may have the potential to bind specifically to the alpha2-I domain in a metal ion-independent fashion.
机译：蛇毒含有许多异源二聚体的C型凝集素样蛋白（CLP），它们与止血系统的成分发生特异性相互作用。来自多刺棘皮蛇毒的EMS16与胶原蛋白受体整联蛋白alpha2beta1（也称为糖蛋白（GP）Ia / IIa）结合，并特异性抑制胶原蛋白结合。在这里，我们报告了与重组整联蛋白α2-I结构域复合的EMS16的晶体结构，该结构在胶原蛋白结合中起着核心作用。该复合物在1.9埃分辨率下的结构表明，α2-I结构域的胶原蛋白结合位点被结合的EMS16完全覆盖。 EMS16的这种阻断似乎在空间上抑制了胶原蛋白与alpha2-I结构域的结合。结合的α2 -I结构域采用闭合构象，这在不存在配体的情况下可见，这表明EMS16稳定了对应于α2 -I结构域的活性较低结构的闭合构象。 EMS16不直接结合至锰离子和alpha2-I结构域的金属离子依赖性粘附位点（MIDAS）的残基，这表明EMS16可能具有与金属离子无关的α2-I结构域特异性结合的潜力时尚。

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