Most yeast SH3 domains bind peptide targets with high intrinsic specificity.

ABSTRACT: A need exists to develop bioinformatics for predicting differences in protein function, especially for members of a domain family who share a common fold, yet are found in a diverse array of proteins. Many domain families have been conserved over large evolutionary spans and representative genomic data during these periods are now available. This allows a simple method for grouping domain sequences to reveal common and unique/specific binding residues. As such, we hypothesize that sequence alignment analysis of the yeast SH3 domain family across ancestral species in the fungal kingdom can determine whether each member encodes specific information to bind unique peptide targets. With this approach, we identify important specific residues for a given domain as those that show little conserva

SUBMITTER: Brown T 

PROVIDER: S-EPMC5823434 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature