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Versatility and invariance in the evolution of homologous heteromeric interfaces.


ABSTRACT: Evolutionary pressures act on protein complex interfaces so that they preserve their complementarity. Nonetheless, the elementary interactions which compose the interface are highly versatile throughout evolution. Understanding and characterizing interface plasticity across evolution is a fundamental issue which could provide new insights into protein-protein interaction prediction. Using a database of 1,024 couples of close and remote heteromeric structural interologs, we studied protein-protein interactions from a structural and evolutionary point of view. We systematically and quantitatively analyzed the conservation of different types of interface contacts. Our study highlights astonishing plasticity regarding polar contacts at complex interfaces. It also reveals that up to a quarter o

SUBMITTER: Andreani J 

PROVIDER: S-EPMC3431345 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature

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