Solution Structure of a Two-repeat Fragment of Major Vault Protein

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DOIResolve DOI: http://doi.org/10.1016/j.jmb.2005.11.064
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TypeArticle
Journal titleJ Mol Biol
Volume356
Issue2
Pages444452; # of pages: 9
Subjectgenome; Human; pha; Protein; Proteins; therapy
AbstractMajor 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
Publication date
AffiliationNRC Biotechnology Research Institute; National Research Council Canada
Peer reviewedNo
NRC number47486
NPARC number3540008
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Record identifier6a591e75-e6a0-4804-b7db-c539bce15eb8
Record created2009-03-01
Record modified2016-05-09
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