PDZ domains: Folding and binding

被引：134

作者：

Jemth, Per

Gianni, Stefano

机构：

[1] Uppsala Univ, Dept Med Biochem, S-75123 Uppsala, Sweden

[2] Univ Roma La Sapienza, CNR, Ist Biol & Patol Mol, Dipartimento Sci Biochim A Rossi Fanelli, I-00185 Rome, Italy

来源：

BIOCHEMISTRY | 2007年 / 46卷 / 30期

关键词：

D O I：

10.1021/bi7008618

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：

The PDZ domain is one of the most common protein-protein interaction domains in humans, and it is found in all kingdoms of life. We will review recent progress in the understanding of biophysical aspects of PDZ domains with emphasis on the folding and binding reactions. Finally, we discuss an intriguing correlation between stability and binding of peptide for PDZ2 from PTP-BL.

引用

页码：8701 / 8708

页数：8

共 63 条

[61] A closed binding pocket and global destabilization modify the binding properties of an alternatively spliced form of the second PDZ domain of PTP-BL [J].