Sequence variation in ligand binding sites in proteins.

ABSTRACT:

Background

The recent explosion in the availability of complete genome sequences has led to the cataloging of tens of thousands of new proteins and putative proteins. Many of these proteins can be structurally or functionally categorized from sequence conservation alone. In contrast, little attention has been given to the meaning of poorly-conserved sites in families of proteins, which are typically assumed to be of little structural or functional importance.

Results

Recently, using statistical free energy analysis of tetratricopeptide repeat (TPR) domains, we observed that positions in contact with peptide ligands are more variable than surface positions in general. Here we show that statistical analysis of TPRs, ankyrin repeats, Cys2His2 zinc fingers and PDZ domains accura

SUBMITTER: Magliery TJ 

PROVIDER: S-EPMC1261162 | biostudies-literature | 2005 Sep

REPOSITORIES: biostudies-literature