A conserved folding mechanism for PDZ domains

被引：43

作者：

Chi, Celestine N.

Gianni, Stefano

Calosci, Nicoletta

Travaglini-Allocatelli, Carlo

Engstrom, Ake

Jemth, Per

机构：

[1] Uppsala Univ, Dept Med Biochem & Microbiol, SE-75123 Uppsala, Sweden

[2] Univ Roma La Sapienza, Dipartimento Sci Biochim A Rossi Fanelli, I-00185 Rome, Italy

[3] Univ Roma La Sapienza, CNR, Ist Biol & Patol Mol, I-00185 Rome, Italy

来源：

FEBS LETTERS | 2007年 / 581卷 / 06期

关键词：

protein folding; folding mechanism; PDZ domain; kinetics;

D O I：

10.1016/j.febslet.2007.02.011

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 protein folding is whether the folding mechanism is sequence dependent and conserved for homologous proteins. In this work we compared the kinetic folding mechanism of five postsynaptic density protein-95, disc-large tumor suppressor protein, zonula occludens-1 (PDZ) domains, sharing similar topology but having different primary structures. Investigation of the different proteins under various experimental conditions revealed that the folding kinetics of each member of the PDZ family can be described by a model with two transition states separated by an intermediate. Moreover, the positions of the two transition states along the reaction coordinate (as given by their PT-values) are fairly constant for the five PDZ domains. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：1109 / 1113

页数：5

共 25 条

[1] Two conserved residues govern the salt and pH dependencies of the binding reaction of a PDZ domain [J].