2CTN

STRUCTURE OF CALCIUM-SATURATED CARDIAC TROPONIN C, NMR, 30 STRUCTURES

2CTN の概要

• エントリーDOI: 10.2210/pdb2ctn/pdb
• 分子名称: TROPONIN C, CALCIUM ION (2 entities in total)
• 機能のキーワード: cardiac, muscle, regulatory, calcium-binding protein
• 由来する生物種: Gallus gallus (chicken)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9974.12

構造登録者

Sia, S.K.,Li, M.X.,Spyracopoulos, L.,Gagne, S.M.,Liu, W.,Putkey, J.A.,Sykes, B.D. (登録日: 1997-05-06, 公開日: 1998-05-06, 最終更新日: 2024-05-22)

主引用文献

Sia, S.K.,Li, M.X.,Spyracopoulos, L.,Gagne, S.M.,Liu, W.,Putkey, J.A.,Sykes, B.D.
Structure of cardiac muscle troponin C unexpectedly reveals a closed regulatory domain.
J.Biol.Chem., 272:18216-18221, 1997

PubMed Abstract: The regulation of cardiac muscle contraction must differ from that of skeletal muscles to effect different physiological and contractile properties. Cardiac troponin C (TnC), the key regulator of cardiac muscle contraction, possesses different functional and Ca2+-binding properties compared with skeletal TnC and features a Ca2+-binding site I, which is naturally inactive. The structure of cardiac TnC in the Ca2+-saturated state has been determined by nuclear magnetic resonance spectroscopy. The regulatory domain exists in a "closed" conformation even in the Ca2+-bound (the "on") state, in contrast to all predicted models and differing significantly from the calcium-induced structure observed in skeletal TnC. This structure in the Ca2+-bound state, and its subsequent interaction with troponin I (TnI), are crucial in determining the specific regulatory mechanism for cardiac muscle contraction. Further, it will allow for an understanding of the action of calcium-sensitizing drugs, which bind to cardiac TnC and are known to enhance the ability of cardiac TnC to activate cardiac muscle contraction.

PubMed: 9218458
DOI: 10.1074/jbc.272.29.18216

実験手法

SOLUTION NMR