Common Patterns in Chaperone Interactions with a Native Client Protein,Angewandte Chemie International Edition

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Common Patterns in Chaperone Interactions with a Native Client Protein
Angewandte Chemie International Edition ( IF 16.1 ) Pub Date : 2018-04-17 , DOI: 10.1002/anie.201713064
Lichun He ₁ , Sebastian Hiller ₁

Affiliation

Many molecular chaperones are promiscuous and interact with a wide range of unfolded, quasi‐native, and native client proteins. The mechanisms by which chaperones interact with the highly diverse structures of native clients thus remain puzzling. In this work, we investigate at the atomic level how three ATP‐independent chaperones interact with a β‐sheet‐rich protein, the Fyn SH3 domain. The results reveal that the chaperone Spy recognizes the locally frustrated surface of the client Fyn SH3 and that the interaction is transient and highly dynamic, leaving the chaperone‐interacting surface on Fyn SH3 solvent accessible. The two alternative molecular chaperones SurA and Skp recognize the same locally frustrated surface of the Fyn SH3 domain. These results indicate dynamic recognition of frustrated segments as a common mechanism underlying the chaperone–native client interaction, which also provides a basis for chaperone promiscuousness.

中文翻译：

伴侣分子与天然客户蛋白相互作用的常见模式。

许多分子伴侣是混杂的，并与多种未折叠的，准天然的和天然的客户蛋白质相互作用。伴侣与本地客户的高度多样化的结构相互作用的机制因此仍然令人困惑。在这项工作中，我们在原子水平上研究了三个不依赖ATP的伴侣如何与富含β-折叠的蛋白Fyn SH3域相互作用。结果表明，伴侣Spy可以识别客户Fyn SH3的局部受挫表面，并且相互作用是短暂且高度动态的，从而使Fyn SH3溶剂上的与伴侣相互作用的表面可访问。两个替代分子伴侣SurA和Skp识别Fyn SH3结构域的相同的局部受挫表面。

更新日期：2018-04-17

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