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1AVS

X-RAY CRYSTALLOGRAPHIC STUDY OF CALCIUM-SATURATED N-TERMINAL DOMAIN OF TROPONIN C

Summary for 1AVS
Entry DOI10.2210/pdb1avs/pdb
DescriptorTROPONIN C, CALCIUM ION (3 entities in total)
Functional Keywordsmuscle contraction, calcium-activated, troponin, e-f hand calcium-binding protein
Biological sourceGallus gallus (chicken)
Total number of polymer chains2
Total formula weight20128.48
Authors
Strynadka, N.C.J.,James, M.N.G. (deposition date: 1997-09-19, release date: 1997-12-24, Last modification date: 2024-05-22)
Primary citationStrynadka, N.C.,Cherney, M.,Sielecki, A.R.,Li, M.X.,Smillie, L.B.,James, M.N.
Structural details of a calcium-induced molecular switch: X-ray crystallographic analysis of the calcium-saturated N-terminal domain of troponin C at 1.75 A resolution.
J.Mol.Biol., 273:238-255, 1997
Cited by
PubMed Abstract: We have solved and refined the crystal and molecular structures of the calcium-saturated N-terminal domain of troponin C (TnC) to 1.75 A resolution. This has allowed for the first detailed analysis of the calcium binding sites of this molecular switch in the calcium-loaded state. The results provide support for the proposed binding order and qualitatively, for the affinity of calcium in the two regulatory calcium binding sites. Based on a comparison with the high-resolution apo-form of TnC we propose a possible mechanism for the calcium-mediated exposure of a large hydrophobic surface that is central to the initiation of muscle contraction within the cell.
PubMed: 9367759
DOI: 10.1006/jmbi.1997.1257
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.75 Å)
Structure validation

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