Persistently conserved positions in structurally similar, sequence dissimilar proteins: roles in preserving protein fold and function.

ABSTRACT: Many protein pairs that share the same fold do not have any detectable sequence similarity, providing a valuable source of information for studying sequence-structure relationship. In this study, we use a stringent data set of structurally similar, sequence-dissimilar protein pairs to characterize residues that may play a role in the determination of protein structure and/or function. For each protein in the database, we identify amino-acid positions that show residue conservation within both close and distant family members. These positions are termed "persistently conserved". We then proceed to determine the "mutually" persistently conserved (MPC) positions: those structurally aligned positions in a protein pair that are persistently conserved in both pair mates. Because of their intra-

SUBMITTER: Friedberg I 

PROVIDER: S-EPMC2373454 | biostudies-literature | 2002 Feb

REPOSITORIES: biostudies-literature