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PDBsum entry 1tnp
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Calcium-binding protein
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PDB id
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1tnp
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References listed in PDB file
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Key reference
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Title
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Structures of the troponin c regulatory domains in the apo and calcium-Saturated states.
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Authors
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S.M.Gagné,
S.Tsuda,
M.X.Li,
L.B.Smillie,
B.D.Sykes.
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Ref.
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Nat Struct Biol, 1995,
2,
784-789.
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PubMed id
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Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above were
obtained from the PDBe's
server.
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Abstract
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Regulation of contraction in skeletal muscle occurs through calcium binding to
the protein troponin C. The solution structures of the regulatory domain of apo
and calcium-loaded troponin C have been determined by multinuclear,
multidimensional nuclear magnetic resonance techniques. The structural
transition in the regulatory domain of troponin C on calcium binding involves an
opening of the structure through large changes in interhelical angles. This
leads to the increased exposure of an extensive hydrophobic patch, an event that
triggers skeletal muscle contraction.
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Secondary reference #1
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Title
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Quantification of the calcium-Induced secondary structural changes in the regulatory domain of troponin-C.
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Authors
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S.M.Gagné,
S.Tsuda,
M.X.Li,
M.Chandra,
L.B.Smillie,
B.D.Sykes.
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Ref.
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Protein Sci, 1994,
3,
1961-1974.
[DOI no: ]
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PubMed id
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Figure 5.
Fig. 5. Schematicrepresentation of the econdary structure determination of NTnC.2Ca. Therepresentation used is the same
as in igure 4, except or theCSI,which s a consensus of the 'Ha, I3Ca, and 13C0 index.
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Figure 9.
Fig. 9. chematicrepresentaton of theCa2+-inducedstraightening of anditspossibleimpactonthetertiaryfold of
NTnC. I: TheCa*+-freecrystalstructure(Herzberg & ames, 988). 1: The predicted Ca2+-satratedstructure(Herzbeg et at.,
1986). 111: Sameas , ith helix-B straightened by changingthe $I/$ backboneangle of 41fro -961-7 to s
canbeseen y omparing 11 and 111, thestraightening of helix-B, which is thepredominantCa2+-inducedsecondarystructure
changeobserved by NMRinNTnC,couldaccountformost of heopening of NTnCuponCa2+ binding.
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The above figures are
reproduced from the cited reference
which is an Open Access publication published by the Protein Society
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