1cta
From Proteopedia
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|PDB= 1cta |SIZE=350|CAPTION= <scene name='initialview01'>1cta</scene> | |PDB= 1cta |SIZE=350|CAPTION= <scene name='initialview01'>1cta</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ctd|1CTD]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cta OCA], [http://www.ebi.ac.uk/pdbsum/1cta PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cta RCSB]</span> | ||
}} | }} | ||
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[[Category: Shaw, G S.]] | [[Category: Shaw, G S.]] | ||
[[Category: Sykes, B D.]] | [[Category: Sykes, B D.]] | ||
| - | [[Category: ACE]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: NH2]] | ||
[[Category: muscle protein]] | [[Category: muscle protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:28:06 2008'' |
Revision as of 16:28, 30 March 2008
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| Ligands: | , , | ||||||
| Related: | 1CTD
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
DETERMINATION OF THE SOLUTION STRUCTURE OF A SYNTHETIC TWO-SITE CALCIUM-BINDING HOMODIMERIC PROTEIN DOMAIN BY NMR SPECTROSCOPY
Overview
The solution structure of a 34-residue synthetic calcium-binding peptide from site III of chicken troponin-C has been determined by 1H NMR spectroscopy. In solution and in the presence of calcium this peptide forms a symmetric two-site homodimeric calcium-binding domain (Shaw et al., 1990). The solution structure of this dimer was determined from the measurement of 470 NOEs from a 75-ms NOESY data set. For the dimer structure determination, the constraint list included 868 distance restraints, 44 phi angles, and 24 chi 1 and 2 chi 2 angles. Seven structures were calculated by restrained molecular dynamics using a procedure in which intramonomer distances were used first and then all distances, intra- and intermonomer, were input during further dynamics. The structures exhibited a fold very similar to the C-terminal domain of troponin-C comprised of a pair of helix-loop-helix calcium-binding sites. The rms deviation of these structures for backbone atoms between residues 97-122 and 97'-122' for the dimer was 0.82 A. The dimer structure was also calculated to be more symmetric than sites III and IV in troponin-C.
About this Structure
1CTA is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Determination of the solution structure of a synthetic two-site calcium-binding homodimeric protein domain by NMR spectroscopy., Shaw GS, Hodges RS, Sykes BD, Biochemistry. 1992 Oct 13;31(40):9572-80. PMID:1390738
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