Thermodynamic contribution of backbone conformational entropy in the binding between SH3 domain and proline-rich motif

被引:7
作者
Zeng, Danyun [1 ]
Shen, Qingliang [1 ]
Cho, Jae-Hyun [1 ]
机构
[1] Texas A&M Univ, Dept Biochem & Biophys, College Stn, TX 77843 USA
关键词
Intrinsically disordered proteins; Conformational entropy; SH3; domain; Proline-rich motif; Protein -protein interactions; INTRINSICALLY DISORDERED PROTEINS; MAGNETIC-RESONANCE RELAXATION; MODEL-FREE APPROACH; II HELIX FORMATION; ORDER PARAMETERS; CHEMICAL-SHIFTS; SPIN-RELAXATION; NMR; PEPTIDES; MACROMOLECULES;
D O I
10.1016/j.bbrc.2017.01.089
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
Biological functions of intrinsically disordered proteins (IDPs), and proteins containing intrinsically disordered regions (IDRs) are often mediated by short linear motifs, like proline-rich motifs (PRMs). Upon binding to their target proteins, IDPs undergo a disorder-to-order transition which is accompanied by a large conformational entropy penalty. Hence, the molecular mechanisms underlying control of conformational entropy are critical for understanding the binding affinity and selectivity of IDPs-mediated protein-protein interactions (PPIs). Here, we investigated the backbone conformational entropy change accompanied by binding of the N-terminal SH3 domain (nSH3) of CrkII and PRM derived from guanine nucleotide exchange factor 1 (C3G). In particular, we focused on the estimation of conformational entropy change of disordered PRM upon binding to the nSH3 domain. Quantitative characterization of conformational dynamics of disordered peptides like PRMs is limited. Hence, we combined various methods, including NMR model-free analysis, (delta 2D, DynaMine, and structure-based calculation of entropy loss. This study demonstrates that the contribution of backbone conformational entropy change is significant in the PPIs mediated by IDPs/IDRs. (C) 2017 Elsevier Inc. All rights reserved.
引用
收藏
页码:21 / 26
页数:6
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