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7SC2

CRYSTAL STRUCTURE OF THE N-DOMAIN OF CARDIAC MUSCLE TROPONIN C TETHERED TO THE SWITCH REGION OF CARDIAC MUSCLE TROPONIN I (TETRAGONAL FORM)

Summary for 7SC2
Entry DOI10.2210/pdb7sc2/pdb
DescriptorTroponin C, slow skeletal and cardiac muscles,Troponin I, cardiac muscle chimera, CALCIUM ION (3 entities in total)
Functional Keywordscalcium sensitizer, contraction regulation, contractile protein, cardiac troponin, muscle regulation, calcium-binding, ef-hand
Biological sourceHomo sapiens (Human)
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Total number of polymer chains1
Total formula weight13340.27
Authors
Sack, J.S. (deposition date: 2021-09-27, release date: 2021-12-01, Last modification date: 2024-05-22)
Primary citationYan, C.,Sack, J.S.
X-ray structure of a human cardiac muscle troponin C/troponin I chimera in two crystal forms.
Acta Crystallogr.,Sect.F, 78:17-24, 2022
Cited by
PubMed Abstract: The X-ray crystal structure of a human cardiac muscle troponin C/troponin I chimera has been determined in two different crystal forms and shows a conformation of the complex that differs from that previously observed by NMR. The chimera consists of the N-terminal domain of troponin C (cTnC; residues 1-80) fused to the switch region of troponin I (cTnI; residues 138-162). In both crystal forms, the cTnI residues form a six-turn α-helix that lays across the hydrophobic groove of an adjacent cTnC molecule in the crystal structure. In contrast to previous models, the cTnI helix runs in a parallel direction relative to the cTnC groove and completely blocks the calcium desensitizer binding site of the cTnC-cTnI interface.
PubMed: 34981771
DOI: 10.1107/S2053230X21012395
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.814 Å)
Structure validation

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