5OB4

NMR spatial structure of HER2 TM domain dimer in DPC micelles.

5OB4 の概要

• エントリーDOI: 10.2210/pdb5ob4/pdb
• NMR情報: BMRB: 34154
• 分子名称: Receptor tyrosine-protein kinase erbB-2 (1 entity in total)
• 機能のキーワード: protein erbb2 her2 receptor tyrosine kinase membrane domain dimer, membrane protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 9469.61

構造登録者

Mineev, K.S.,Arseniev, A.S. (登録日: 2017-06-26, 公開日: 2017-11-22, 最終更新日: 2024-06-19)

主引用文献

Lesovoy, D.M.,Mineev, K.S.,Bragin, P.E.,Bocharova, O.V.,Bocharov, E.V.,Arseniev, A.S.
NMR relaxation parameters of methyl groups as a tool to map the interfaces of helix-helix interactions in membrane proteins.
J. Biomol. NMR, 69:165-179, 2017

PubMed Abstract: In the case of soluble proteins, chemical shift mapping is used to identify the intermolecular interfaces when the NOE-based calculations of spatial structure of the molecular assembly are impossible or impracticable. However, the reliability of the membrane protein interface mapping based on chemical shifts or other relevant parameters was never assessed. In the present work, we investigate the predictive power of various NMR parameters that can be used for mapping of helix-helix interfaces in dimeric TM domains. These parameters are studied on a dataset containing three structures of helical dimers obtained for two different proteins in various membrane mimetics. We conclude that the amide chemical shifts have very little predictive value, while the methyl chemical shifts could be used to predict interfaces, though with great care. We suggest an approach based on conversion of the carbon NMR relaxation parameters of methyl groups into parameters of motion, and one of such values, the characteristic time of methyl rotation, appears to be a reliable sensor of interhelix contacts in transmembrane domains. The carbon NMR relaxation parameters of methyl groups can be measured accurately and with high sensitivity and resolution, making the proposed parameter a useful tool for investigation of protein-protein interfaces even in large membrane proteins. An approach to build the models of transmembrane dimers based on perturbations of methyl parameters and TMDOCK software is suggested.

PubMed: 29063258
DOI: 10.1007/s10858-017-0146-1

実験手法

SOLUTION NMR