Heterotypic Coiled-Coil Formation is Essential for the Correct Assembly of the Septin Heterofilament.

ABSTRACT: Protein-protein interactions play a critical role in promoting the stability of protein quaternary structure and in the assembly of large macromolecular complexes. What drives the stabilization of such assemblies is a central question in biology. A limiting factor in fully understanding such systems is the transient nature of many complexes, making structural studies difficult. Septins comprise a conserved family of guanine nucleotide binding proteins that polymerize in the form of heterofilaments. In structural terms, they have a common organization: a central GTPase domain, an N-terminal domain, and a C-terminal domain; the latter is predicted to form a coiled coil. Currently, even for the best characterized human septin heterocomplex (SEPT2/SEPT6/SEPT7), the role of C-terminal domain is

SUBMITTER: Sala FA 

PROVIDER: S-EPMC5192694 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature