1y7x
From Proteopedia
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Solution structure of a two-repeat fragment of major vault protein
Contents |
Overview
Major vault protein (MVP) is the main constituent of vaults, large, ribonucleoprotein particles implicated in resistance to cancer therapy and, correlated with poor survival prognosis. Here, we report the structure of, the main repeat element in human MVP. The approximately 55 amino acid, residue MVP domain has a unique, novel fold that consists of a, three-stranded antiparallel beta-sheet. The solution NMR structure of a, two-domain fragment reveals the interdomain contacts and relative, orientations of the two MVP domains. We use these results to model the, assembly of 672 MVP domains from 96 MVP molecules into the ribs of the, 13MDa vault structure. The unique features include a thin, skin-like, structure with polar residues on both the cytoplasmic and internal, surface, and a pole-to-pole arrangement of MVP molecules. These studies, provide a starting point for understanding the self-assembly of MVP into, vaults and their interactions with other proteins. Chemical shift, perturbation studies identified the binding site of vault poly(ADP-ribose), polymerase, another component of vault particles, indicating that MVP, domains form a new class of interaction-mediating modules.
Disease
Known diseases associated with this structure: Leigh syndrome, French-Canadian type OMIM:[607544], Mitral valve prolapse, myxomatous 1 OMIM:[157700]
About this Structure
1Y7X is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of a two-repeat fragment of major vault protein., Kozlov G, Vavelyuk O, Minailiuc O, Banville D, Gehring K, Ekiel I, J Mol Biol. 2006 Feb 17;356(2):444-52. Epub 2005 Dec 7. PMID:16373071
Page seeded by OCA on Mon Nov 12 20:15:57 2007
