Combining specificity determining and conserved residues improves functional site prediction.

ABSTRACT:

Background

Predicting the location of functionally important sites from protein sequence and/or structure is a long-standing problem in computational biology. Most current approaches make use of sequence conservation, assuming that amino acid residues conserved within a protein family are most likely to be functionally important. Most often these approaches do not consider many residues that act to define specific sub-functions within a family, or they make no distinction between residues important for function and those more relevant for maintaining structure (e.g. in the hydrophobic core). Many protein families bind and/or act on a variety of ligands, meaning that conserved residues often only bind a common ligand sub-structure or perform general catalytic activities.

Results<

SUBMITTER: Kalinina OV 

PROVIDER: S-EPMC2709924 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature