Conserved signature proposed for folding in the lipocalin superfamily.
We systematically identify a group of evolutionarily conserved residues proposed for folding in a model beta-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 beta-lactoglobulin, suggest that the evolutionarily conserved regions fold on a faster folding time-scale than the non-conserved regions.
Greene
Lesley H
LH
Department of Biochemistry and Molecular Biology, University of Miami School of Medicine, Miami, FL 33101, USA. lesley.greene@bioch.ox.ac.uk
Hamada
Daizo
D
Eyles
Stephen J
SJ
Brew
Keith
K
D002942:Circular Dichroism; D017124:Conserved Sequence; D006801:Humans; D007700:Kinetics; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D012177:Retinol-Binding Proteins / Q000737:chemistry* / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013329:Structure-Activity Relationship
D012177:Retinol-Binding Proteins