Conserved signature proposed for folding in the lipocalin superfamily

FEBS Letters

Greene, Lesley H²  Hamada, Daizo³  Eyles, Stephen J¹  Brew, Keith² 

[1] Department of Chemistry, University of Massachusetts at Amherst, Amherst, MA 01003, USA;Department of Biochemistry and Molecular Biology, University of Miami School of Medicine, Miami, FL 33101, USA;Oxford Centre for Molecular Sciences, Central Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QH, UK

关键词: Evolution;    Protein folding;    Conserved residue;    Lipocalin superfamily;    Retinol-binding protein;    β-Lactoglobulin;   

DOI  :  10.1016/S0014-5793(03)00925-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We systematically identify a group of evolutionarily conserved residues proposed for folding in a model β-barrel superfamily, the lipocalins. The nature of conservation at the structural level is defined and we show that the conserved residues are involved in a network of interactions that form the core of the fold. Exploratory kinetic studies are conducted with a model superfamily member, human serum retinol-binding protein, to examine their role. The present results, coupled with key experimental studies conducted with another lipocalin β-lactoglobulin, suggest that the evolutionarily conserved regions fold on a faster folding time-scale than the non-conserved regions.

【 授权许可】

Unknown