Key result
Photo-cross-linking identifies TnI Met121 as the TnC interaction site that moves away slightly without Ca2+.
Population
Rabbit skeletal muscle troponin-C mutants and troponin-I in binary, ternary complexes, and synthetic thin…
Comparison
Photo-cross-linking with benzophenone-4-iodoaceta… vs Presence vs absence of Ca2+
Design
Preclinical
Authors
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Offers structural basis for troponin Ca2+ sensing; leaves open effects on contractility in vivo.
The study identifies TnI Met121 as the contact site for the N-terminal hydrophobic patch of TnC, providing structural insights into Ca2+ regulation in muscle contraction.
Luo et al. (1999) studied this question. TnC mutants with photoactivatable cross-linker was evaluated on Cross-linking site identification. Photo-cross-linking of TnC mutants identified TnI Met121 as the interaction site with the N-terminal hydrophobic patch of TnC, which moves away slightly in the absence of Ca2+.
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