Ligand binding by TPR domains

被引：83

作者：

Cortajarena, AL

Regan, L

机构：

[1] Yale Univ, Dept Chem, New Haven, CT 06520 USA

[2] Yale Univ, Dept Mol Biophys & Biochem, New Haven, CT 06520 USA

来源：

PROTEIN SCIENCE | 2006年 / 15卷 / 05期

关键词：

tetratricopeptide repeat ( TPR); Hsp90; protein phosphatase 5 ( PP5); Vpu-binding protein/small glutamine-rich protein (UBP/SGT); ligand binding;

D O I：

10.1110/ps.062092506

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Tetratricopeptide repeat (TPR) domains bind specific peptide ligands and are thought to mediate protein-protein interactions in a variety of biological systems. Here we compare peptide ligand-binding by several different TPR domains. We present specific examples that demonstrate that TPR domains typically undergo little or no structural rearrangement upon ligand binding. Our data suggest that, contrary to a recent proposal, coupled folding and binding is not the common mechanism of ligand recognition by TPR domains.

引用

收藏

页码：1193 / 1198

页数：6

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