Structural and Thermodynamic Properties of Septin 3 Investigated by Small-Angle X-Ray Scattering.

ABSTRACT: Septins comprise a family of proteins involved in a variety of cellular processes and related to several human pathologies. They are constituted by three structural domains: the N- and C-terminal domains, highly variable in length and composition, and the central domain, involved in the guanine nucleotide (GTP) binding. Thirteen different human septins are known to form heterogeneous complexes or homofilaments, which are stabilized by specific interactions between the different interfaces present in the domains. In this work, we have investigated by in-solution small-angle x-ray scattering the structural and thermodynamic properties of a human septin 3 construct, SEPT3-GC, which contains both of both interfaces (G and NC) responsible for septin-septin interactions. In order to shed light o

SUBMITTER: Ortore MG 

PROVIDER: S-EPMC4472041 | biostudies-literature | 2015 Jun

REPOSITORIES: biostudies-literature