1cta
From Proteopedia
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| - | [[Image:1cta.gif|left|200px]]< | + | [[Image:1cta.gif|left|200px]] |
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| - | '''DETERMINATION OF THE SOLUTION STRUCTURE OF A SYNTHETIC TWO-SITE CALCIUM-BINDING HOMODIMERIC PROTEIN DOMAIN BY NMR SPECTROSCOPY''' | + | {{Structure |
| + | |PDB= 1cta |SIZE=350|CAPTION= <scene name='initialview01'>1cta</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> and <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''DETERMINATION OF THE SOLUTION STRUCTURE OF A SYNTHETIC TWO-SITE CALCIUM-BINDING HOMODIMERIC PROTEIN DOMAIN BY NMR SPECTROSCOPY''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CTA is a [ | + | 1CTA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CTA OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/1390738 1390738] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Shaw, G S.]] | [[Category: Shaw, G S.]] | ||
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[[Category: muscle protein]] | [[Category: muscle protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:28:41 2008'' |
Revision as of 08:28, 20 March 2008
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| Ligands: | , and | ||||||
| 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
Page seeded by OCA on Thu Mar 20 10:28:41 2008
Categories: Single protein | Shaw, G S. | Sykes, B D. | ACE | CA | NH2 | Muscle protein
