2MQ0

NMR structure of the c3 domain of human cardiac myosin binding protein-c

2MQ0 の概要

• エントリーDOI: 10.2210/pdb2mq0/pdb
• 関連するPDBエントリー: 2MQ3
• NMR情報: BMRB: 25007
• 分子名称: Myosin-binding protein C, cardiac-type (1 entity in total)
• 機能のキーワード: cardiac myosin binding protein c, c3 domain, ig-like, hypertrophic cardiomyopathy, contractile protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10827.32

構造登録者

Zhang, X.,De, S.,Mcintosh, L.P.,Paetzel, M. (登録日: 2014-06-10, 公開日: 2014-07-30, 最終更新日: 2024-05-15)

主引用文献

Zhang, X.L.,De, S.,McIntosh, L.P.,Paetzel, M.
Structural Characterization of the C3 Domain of Cardiac Myosin Binding Protein C and Its Hypertrophic Cardiomyopathy-Related R502W Mutant.
Biochemistry, 53:5332-5342, 2014

PubMed Abstract: Human cardiac myosin binding protein C (cMyBP-C), a thick filament protein found within the sarcomere of cardiac muscle, regulates muscle contraction and is essential for proper muscle function. Hypertrophic cardiomyopathy (HCM), a genetic disease affecting 1 in 500 people, is the major cause of death in young athletes. It is caused by genetic mutations within sarcomeric proteins. Forty-two percent of the HCM-related mutations are found in cMyBP-C. Here we present the nuclear magnetic resonance-derived structural ensembles of the wild-type cMyBP-C C3 domain and its HCM-related R502W mutant. The C3 domain adopts an immunoglobulin-like fold, and mutation of the exposed Arg502 to a tryptophan does not perturb its structure, dynamics, or stability. However, the R502W mutation does alter the predicted electrostatic properties of the C3 domain. We hypothesize that this mutation, and other HCM-linked mutations found within the same domain, may directly disrupt the interaction of cMyBP-C with other sarcomeric proteins.

PubMed: 25058872
DOI: 10.1021/bi500784g

実験手法

SOLUTION NMR