Probing large conformational rearrangements in wild-type and mutant spectrin using structural mass spectrometry.

ABSTRACT: Conformational changes of macromolecular complexes play key mechanistic roles in many biological processes, but large, highly flexible proteins and protein complexes usually cannot be analyzed by crystallography or NMR. Here, structures and conformational changes of the highly flexible, dynamic red cell spectrin and effects of a common mutation that disrupts red cell membranes were elucidated using chemical cross-linking coupled with mass spectrometry. Interconversion of spectrin between closed dimers, open dimers, and tetramers plays a key role in maintaining red cell shape and membrane integrity, and spectrins in other cell types serve these as well as more diverse functions. Using a minispectrin construct, experimentally verified structures of closed dimers and tetramers were determined

SUBMITTER: Sriswasdi S 

PROVIDER: S-EPMC3918770 | biostudies-literature | 2014 Feb

REPOSITORIES: biostudies-literature