Analyses on clustering of the conserved residues at protein-RNA interfaces and its application in binding site identification.

ABSTRACT:

Background

The maintenance of protein structural stability requires the cooperativity among spatially neighboring residues. Previous studies have shown that conserved residues tend to occur clustered together within enzyme active sites and protein-protein/DNA interfaces. It is possible that conserved residues form one or more local clusters in protein tertiary structures as it can facilitate the formation of functional motifs. In this work, we systematically investigate the spatial distributions of conserved residues as well as hot spot ones within protein-RNA interfaces.

Results

The analysis of 191 polypeptide chains from 160 complexes shows the polypeptides interacting with tRNAs evolve relatively rapidly. A statistical analysis of residues in different regions shows that

SUBMITTER: Yang Z 

PROVIDER: S-EPMC7027071 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature