1ctd: Difference between revisions

Revision as of 13:09, 21 February 2008

DETERMINATION OF THE SOLUTION STRUCTURE OF A SYNTHETIC TWO-SITE CALCIUM-BINDING HOMODIMERIC PROTEIN DOMAIN BY NMR SPECTROSCOPY

OverviewOverview

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 StructureAbout this Structure

1CTD is a Single protein structure of sequence from [1] with , and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1ctd.jpg|left|200px]]<br /><applet load="1ctd" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1ctd.jpg|left|200px]]<br /><applet load="1ctd" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1ctd" />
 '''DETERMINATION OF THE SOLUTION STRUCTURE OF A SYNTHETIC TWO-SITE CALCIUM-BINDING HOMODIMERIC PROTEIN DOMAIN BY NMR SPECTROSCOPY'''<br />
 ==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.
+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==
-CTD 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CTD OCA].
+CTD 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=1CTD 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1390738 1390738]
 [[Category: Single protein]]
-[[Category: Shaw, G.S.]]
+[[Category: Shaw, G S.]]
-[[Category: Sykes, B.D.]]
+[[Category: Sykes, B D.]]
 [[Category: ACE]]
 [[Category: CA]]
@@ Line 19: / Line 19: @@
 [[Category: muscle protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:56:17 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:09:30 2008''