Evolving specificity from variability for protein interaction domains

被引:36
作者
Kaneko, Tomonori [1 ,2 ]
Sidhu, Sachdev S. [3 ,4 ]
Li, Shawn S. C. [1 ,2 ]
机构
[1] Univ Western Ontario, Dept Biochem, London, ON N6A 5C1, Canada
[2] Univ Western Ontario, Schulich Sch Med & Dent, Siebens Drake Res Inst, London, ON N6A 5C1, Canada
[3] Univ Toronto, Donnelly Ctr, Banting & Best Dept Med Res, Toronto, ON M5S 3E1, Canada
[4] Univ Toronto, Donnelly Ctr, Dept Mol Genet, Toronto, ON M5S 3E1, Canada
基金
加拿大健康研究院;
关键词
ITK SH2 DOMAIN; AFFINITY PHOSPHOTYROSYL PEPTIDE; SRC HOMOLOGY-2 DOMAIN; STRUCTURAL BASIS; PDZ-DOMAIN; BINDING-SITE; RECOGNITION DOMAINS; SIGNAL-TRANSDUCTION; CRYSTAL-STRUCTURES; PHOSPHOPEPTIDE;
D O I
10.1016/j.tibs.2010.12.001
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
An important question in modular domain-peptide interactions, which play crucial roles in many biological processes, is how the diverse specificities exhibited by different members of a domain family are encoded in a common scaffold. Analysis of the Src homology (SH) 2 family has revealed that its specificity is determined, in large part, by the configuration of surface loops that regulate ligand access to binding pockets. In a distinct manner, SH3 domains employ loops for ligand recognition. The PDZ domain, in contrast, achieves specificity by co-evolution of binding-site residues. Thus, the conformational and sequence variability afforded by surface loops and binding sites provides a general mechanism by which to encode the wide spectrum of specificities observed for modular protein interaction domains.
引用
收藏
页码:183 / 190
页数:8
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