Interaction preferences across protein-protein interfaces of obligatory and non-obligatory components are different.

ABSTRACT:

Background

A polypeptide chain of a protein-protein complex is said to be obligatory if it is bound to another chain throughout its functional lifetime. Such a chain might not adopt the native fold in the unbound form. A non-obligatory polypeptide chain associates with another chain and dissociates upon molecular stimulus. Although conformational changes at the interaction interface are expected, the overall 3-D structure of the non-obligatory chain is unaltered. The present study focuses on protein-protein complexes to understand further the differences between obligatory and non-obligatory interfaces.

Results

A non-obligatory chain in a complex of known 3-D structure is recognized by its stable existence with same fold in the bound and unbound forms. On the contrary, an ob

SUBMITTER: De S 

PROVIDER: S-EPMC1201154 | biostudies-literature | 2005 Aug

REPOSITORIES: biostudies-literature