1Y7X

Solution structure of a two-repeat fragment of major vault protein

1Y7X の概要

• エントリーDOI: 10.2210/pdb1y7x/pdb
• NMR情報: BMRB: 6447
• 分子名称: Major vault protein (1 entity in total)
• 機能のキーワード: structural repeats, beta-sheet modules, structural protein, protein binding
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q14764
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12772.56

構造登録者

Kozlov, G.,Vavelyuk, O.,Minailiuc, O.,Banville, D.,Gehring, K.,Ekiel, I. (登録日: 2004-12-10, 公開日: 2005-12-20, 最終更新日: 2024-05-22)

主引用文献

Kozlov, G.,Vavelyuk, O.,Minailiuc, O.,Banville, D.,Gehring, K.,Ekiel, I.
Solution structure of a two-repeat fragment of major vault protein.
J.Mol.Biol., 356:444-452, 2006

PubMed Abstract: 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.

PubMed: 16373071
DOI: 10.1016/j.jmb.2005.11.064

実験手法

SOLUTION NMR