Protein-protein interactions in clathrin vesicular assembly: radial distribution of evolutionary constraints in interfaces.

ABSTRACT: In eukaryotic organisms clathrin-coated vesicles are instrumental in the processes of endocytosis as well as intracellular protein trafficking. Hence, it is important to understand how these vesicles have evolved across eukaryotes, to carry cargo molecules of varied shapes and sizes. The intricate nature and functional diversity of the vesicles are maintained by numerous interacting protein partners of the vesicle system. However, to delineate functionally important residues participating in protein-protein interactions of the assembly is a daunting task as there are no high-resolution structures of the intact assembly available. The two cryoEM structures closely representing intact assembly were determined at very low resolution and provide positions of Cα atoms alone. In the present stud

SUBMITTER: Gadkari RA 

PROVIDER: S-EPMC3285160 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature