2RQM

NMR Solution Structure of Mesoderm Development (MESD) - open conformation

2RQM の概要

• エントリーDOI: 10.2210/pdb2rqm/pdb
• 関連するPDBエントリー: 2RQK
• 分子名称: Mesoderm development candidate 2 (1 entity in total)
• 機能のキーワード: chaperone
• 由来する生物種: Mus musculus (mouse)
• 細胞内の位置: Endoplasmic reticulum: Q9ERE7
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16148.11

構造登録者

Koehler, C.,Lighthouse, J.K.,Werther, T.,Andersen, O.M.,Diehl, A.,Schmieder, P.,Holdener, B.C.,Oschkinat, H. (登録日: 2009-08-14, 公開日: 2009-08-25, 最終更新日: 2024-05-01)

主引用文献

Kohler, C.,Lighthouse, J.K.,Werther, T.,Andersen, O.M.,Diehl, A.,Schmieder, P.,Du, J.,Holdener, B.C.,Oschkinat, H.
The Structure of MESD45-184 Brings Light into the Mechanism of LDLR Family Folding
Structure, 19:337-348, 2011

PubMed Abstract: Mesoderm development (MESD) is a 224 amino acid mouse protein that acts as a molecular chaperone for the low-density lipoprotein receptor (LDLR) family. Here, we provide evidence that the region 45-184 of MESD is essential and sufficient for this function and suggest a model for its mode of action. NMR studies reveal a β-α-β-β-α-β core domain with an α-helical N-terminal extension that interacts with the β sheet in a dynamic manner. As a result, the structural ensemble contains open (active) and closed (inactive) forms, allowing for regulation of chaperone activity through substrate binding. The mutant W61R, which is lethal in Drosophila, adopts only the open state. The receptor motif recognized by MESD was identified by in vitro-binding studies. Furthermore, in vivo functional evidence for the relevance of the identified contact sites in MESD is provided.

PubMed: 21397185
DOI: 10.1016/j.str.2010.12.022

実験手法

SOLUTION NMR