Sequence conservation in lg-like domains: The role of highly conserved proline residues in the fibronectin type III superfamily

被引：78

作者：

Steward, A ^{[1
]}

Adhya, S ^{[1
]}

Clarke, J ^{[1
]}

机构：

[1] Univ Cambridge, Chem Lab, MRC, Ctr Prot Engn, Cambridge CB2 1EW, England

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2002年 / 318卷 / 04期

基金：

英国惠康基金;

关键词：

fibronectin type III; proline; protein stability; protein folding; domain-domain interactions;

D O I：

10.1016/S0022-2836(02)00184-5

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 role of conserved proline residues in fibronectin type III (fnIII) domains is investigated. Surprisingly, none of the standard set of explanations for residue conservation applies. The proline residues are not apparently conserved for function, or stability, or to nucleate folding, or to promote stabilising interactions across domain boundaries. However, when the most highly conserved proline residues are mutated to alanine there is an increase in the rate of aggregation of a fnlll double-module construct. The results suggest that proline residues may be conserved at domain-domain boundaries in fnIII domains to prevent aggregation in multi-modular proteins. (C) 2002 Elsevier Science Ltd. All rights reserved.

引用

页码：935 / 940

页数：6

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