Weak conservation of structural features in the interfaces of homologous transient protein-protein complexes.

ABSTRACT: Residue types at the interface of protein-protein complexes (PPCs) are known to be reasonably well conserved. However, we show, using a dataset of known 3-D structures of homologous transient PPCs, that the 3-D location of interfacial residues and their interaction patterns are only moderately and poorly conserved, respectively. Another surprising observation is that a residue at the interface that is conserved is not necessarily in the interface in the homolog. Such differences in homologous complexes are manifested by substitution of the residues that are spatially proximal to the conserved residue and structural differences at the interfaces as well as differences in spatial orientations of the interacting proteins. Conservation of interface location and the interaction pattern at the c

SUBMITTER: Sudha G 

PROVIDER: S-EPMC4622218 | biostudies-literature | 2015 Nov

REPOSITORIES: biostudies-literature