1cta
From Proteopedia
(New page: 200px<br /><applet load="1cta" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cta" /> '''DETERMINATION OF THE SOLUTION STRUCTURE OF A...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1cta.gif|left|200px]]<br /><applet load="1cta" size=" | + | [[Image:1cta.gif|left|200px]]<br /><applet load="1cta" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1cta" /> | caption="1cta" /> | ||
'''DETERMINATION OF THE SOLUTION STRUCTURE OF A SYNTHETIC TWO-SITE CALCIUM-BINDING HOMODIMERIC PROTEIN DOMAIN BY NMR SPECTROSCOPY'''<br /> | '''DETERMINATION OF THE SOLUTION STRUCTURE OF A SYNTHETIC TWO-SITE CALCIUM-BINDING HOMODIMERIC PROTEIN DOMAIN BY NMR SPECTROSCOPY'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The solution structure of a 34-residue synthetic calcium-binding peptide | + | 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== | ==About this Structure== | ||
| - | 1CTA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with CA, ACE and NH2 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1CTA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=1390738 1390738] | 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=1390738 1390738] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Shaw, G | + | [[Category: Shaw, G S.]] |
| - | [[Category: Sykes, B | + | [[Category: Sykes, B D.]] |
[[Category: ACE]] | [[Category: ACE]] | ||
[[Category: CA]] | [[Category: CA]] | ||
| Line 19: | Line 19: | ||
[[Category: muscle protein]] | [[Category: muscle protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:09:30 2008'' |
Revision as of 10:09, 21 February 2008
|
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] with , and as ligands. 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 Feb 21 12:09:30 2008
Categories: Single protein | Shaw, G S. | Sykes, B D. | ACE | CA | NH2 | Muscle protein
