Cross-linking of residue 57 in the regulatory domain of a mutant rabbit skeletal muscle troponin C to the inhibitory region of troponin I
Population
Mutant rabbit skeletal muscle troponin C (TnC57) and troponin I (TnI)
Design
Preclinical
Authors
Discussion
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Member takes
Implication
No immediate clinical implications; challenges crystal structures by suggesting compact troponin conformation.
Structured PICO
P
Population
Mutant rabbit skeletal muscle troponin C (TnC57) and troponin I (TnI)
I
Intervention
Photoreactive cross-linking with 4-maleimidobenzophenone (BP-Mal) followed by photolysis and peptide sequencing
O
Outcome
Identification of interaction sites between the N-terminal regulatory domain of TnC and the inhibitory region of TnIsurrogate
The study demonstrates that both the C- and N-terminal domains of troponin C interact with the inhibitory region of troponin I, suggesting a more compact conformation of TnC in complex with TnI than observed in crystal structures.
Cite This Study
Kobayashi et al. (1991) studied this question.