3GF5

Crystal structure of the P21 R1-R7 N-terminal domain of murine MVP

3GF5 の概要

• エントリーDOI: 10.2210/pdb3gf5/pdb
• 関連するPDBエントリー: 3GNF 3GNG
• 分子名称: Major vault protein, GLYCEROL (3 entities in total)
• 機能のキーワード: beta sheets, phosphoprotein, ribonucleoprotein, structural protein
• 由来する生物種: Mus musculus (mouse)
• 細胞内の位置: Cytoplasm: Q9EQK5
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 88116.21

構造登録者

Querol-Audi, J.,Casanas, A.,Luque, D.,Caston, J.R.,Fita, I.,Verdaguer, N. (登録日: 2009-02-26, 公開日: 2009-11-10, 最終更新日: 2024-03-20)

主引用文献

Querol-Audi, J.,Casanas, A.,Uson, I.,Luque, D.,Caston, J.R.,Fita, I.,Verdaguer, N.
The mechanism of vault opening from the high resolution structure of the N-terminal repeats of MVP
Embo J., 28:3450-3457, 2009

PubMed Abstract: Vaults are ubiquitous ribonucleoprotein complexes involved in a diversity of cellular processes, including multidrug resistance, transport mechanisms and signal transmission. The vault particle shows a barrel-shaped structure organized in two identical moieties, each consisting of 39 copies of the major vault protein MVP. Earlier data indicated that vault halves can dissociate at acidic pH. The crystal structure of the vault particle solved at 8 A resolution, together with the 2.1-A structure of the seven N-terminal domains (R1-R7) of MVP, reveal the interactions governing vault association and provide an explanation for a reversible dissociation induced by low pH. The structural comparison with the recently published 3.5 A model shows major discrepancies, both in the main chain tracing and in the side chain assignment of the two terminal domains R1 and R2.

PubMed: 19779459
DOI: 10.1038/emboj.2009.274

実験手法

X-RAY DIFFRACTION (2.5 Å)