6SCW

SH3-subunit of chicken alpha spectrin solved by NMR

6SCW の概要

• エントリーDOI: 10.2210/pdb6scw/pdb
• NMR情報: BMRB: 34420
• 分子名称: Spectrin alpha chain, non-erythrocytic 1 isoform X11 (1 entity in total)
• 機能のキーワード: beta-barrel, binding-domain, membrane-ancor, spectrin, peptide binding protein
• 由来する生物種: Sus scrofa (Pig)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7229.24

構造登録者

Grohe, K.,Hebrank, C.,Linser, R. (登録日: 2019-07-25, 公開日: 2020-08-12, 最終更新日: 2024-01-31)

主引用文献

Grohe, K.,Patel, S.,Hebrank, C.,Medina, S.,Klein, A.,Rovo, P.,Vasa, S.K.,Singh, H.,Vogeli, B.,Schafer, L.V.,Linser, R.
Protein Motional Details Revealed by Complementary Structural Biology Techniques.
Structure, 28:1024-, 2020

PubMed Abstract: Proteins depend on defined molecular plasticity for their functionality. How to comprehensively capture dynamics correctly is of ubiquitous biological importance. Approaches commonly used to probe protein dynamics include model-free elucidation of site-specific motion by NMR relaxation, molecular dynamics (MD)-based approaches, and capturing the substates within a dynamic ensemble by recent eNOE-based multiple-structure approaches. Even though MD is sometimes combined with ensemble-averaged NMR restraints, these approaches have largely been developed and used individually. Owing to the different underlying concepts and practical requirements, it has remained unclear how they compare, and how they cross-validate and complement each other. Here, we extract and compare the differential information contents of MD simulations, NMR relaxation measurements, and eNOE-based multi-state structures for the SH3 domain of chicken α-spectrin. The data show that a validated, consistent, and detailed picture is feasible both for timescales and actual conformational states sampled in the dynamic ensemble. This includes the biologically important side-chain plasticity, for which experimentally cross-validated assessment is a significant challenge.

PubMed: 32579946
DOI: 10.1016/j.str.2020.06.001

実験手法

SOLUTION NMR