Role of the structural domain of troponin C in muscle regulation: NMR studies of Ca2+ binding and subsequent interactions with regions 1-40 and 96-115 of troponin I.

Abstract:

:The interaction between the calcium binding and inhibitory components of troponin is central to the regulation of muscle contraction. In this work, two-dimensional heteronuclear single-quantum coherence nuclear magnetic resonance (2D-¿1H,15N¿-HSQC NMR) spectroscopy was used to determine the stoichiometry, affinity, and mechanisms for binding of Ca2+ and two synthetic TnI peptides [TnI1-40 (or Rp40) and TnI96-115] to the isolated C-domain of skeletal troponin C (CTnC). The Ca2+ titration revealed that 2 equiv of Ca2+ binds to sites III and IV of CTnC with strong positive cooperativity and high affinity [dissociation constant (KD)

journal_name

Biochemistry

journal_title

Biochemistry

authors

Mercier P,Li MX,Sykes BD

doi

10.1021/bi992579n

subject

Has Abstract

pub_date

2000-03-21 00:00:00

pages

2902-11

issue

11

eissn

0006-2960

issn

1520-4995

pii

bi992579n

journal_volume

39

pub_type

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