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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >SPECIFIC INTERACTIONS OUTSIDE THE PROLINE-RICH CORE OF TWO CLASSES OF SRC HOMOLOGY 3 LIGANDS
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SPECIFIC INTERACTIONS OUTSIDE THE PROLINE-RICH CORE OF TWO CLASSES OF SRC HOMOLOGY 3 LIGANDS

机译：两类SRC同源3种配体的富含脯氨酸的核心之间的特定相互作用

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摘要

Two dodecapeptides belonging to distinct classes of Src homology 3 (SH3) ligands and selected from biased phage display libraries were used to investigate interactions between a specificity pocket in the Src SH3 domain and ligand residues flanking the proline-rich core, The solution structures of c-Src SH3 complexed with these peptides were solved by NMR. In addition to a proline-rich, polyproline type II helix-forming core, the class I and II ligands each possesses a flanking sequence that occupies a large pocket between the RT and n-Src loops of the SH3 domain. Structural and mutational analyses illustrate how the two classes of SH3 ligands exploit a specificity pocket on the receptor differently to increase binding affinity and specificity.
机译：使用两个偏肽分别属于Src同源3（SH3）配体的不同类别并从有偏倚的噬菌体展示文库中进行选择，以研究Src SH3域中的特异性口袋与富含脯氨酸的核心侧翼的配体残基之间的相互作用。与这些肽复合的-Src SH3通过NMR解析。除了富含脯氨酸，聚脯氨酸的II型螺旋形成核心外，I类和II类配体各自具有侧翼序列，该侧翼序列在SH3结构域的RT和n-Src环之间占据了很大的口袋。结构和突变分析说明了这两类SH3配体如何不同地利用受体上的特异性口袋来增加结合亲和力和特异性。

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