Structural analysis of influenza A virus matrix protein M1 and its self-assemblies at low pH.

ABSTRACT: Influenza A virus matrix protein M1 is one of the most important and abundant proteins in the virus particles broadly involved in essential processes of the viral life cycle. The absence of high-resolution data on the full-length M1 makes the structural investigation of the intact protein particularly important. We employed synchrotron small-angle X-ray scattering (SAXS), analytical ultracentrifugation and atomic force microscopy (AFM) to study the structure of M1 at acidic pH. The low-resolution structural models built from the SAXS data reveal a structurally anisotropic M1 molecule consisting of a compact NM-fragment and an extended and partially flexible C-terminal domain. The M1 monomers co-exist in solution with a small fraction of large clusters that have a layered architecture simil

SUBMITTER: Shtykova EV 

PROVIDER: S-EPMC3865061 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature