1ocp: Difference between revisions

Revision as of 15:16, 21 February 2008

SOLUTION STRUCTURE OF OCT3 POU-HOMEODOMAIN

OverviewOverview

The POU-homeodomain (POUH) forms the bipartite DNA-binding POU domain in association with the POU-specific domain. The 1H, 15N, and 13C magnetic resonances of the 67-amino acid long POUH of mouse Oct-3 have almost completely been assigned, mainly through the combined use of three-dimensional triple resonance NMR methods. Based on the distance and dihedral angle constraints derived from the NMR data, the solution structure of the POUH domain has been calculated by the ab initio simulated annealing method. The average RMS deviation for all backbone heavy atoms of the 20 best calculated structures for residues 9-53 of the total 67 amino acid residues is 0.44 A. The POUH domain consists of three alpha-helices (helix-I, 10-20; helix-II, 28-38; and helix-III, 42-53), and helices-II and -III form a helix-turn-helix motif. In comparison with other classical homeodomains, the folding of the three helices is quite similar. However, the length of helix-III is fairly short. In the complex of the Oct-1 POU domain with an octamer site (Klemm JD, et al., 1994, Cell 77:21-32), the corresponding region is involved in helix-III. The structural difference between these two cases will be discussed.

About this StructureAbout this Structure

1OCP is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the Oct-3 POU-homeodomain in solution, as determined by triple resonance heteronuclear multidimensional NMR spectroscopy., Morita EH, Shirakawa M, Hayashi F, Imagawa M, Kyogoku Y, Protein Sci. 1995 Apr;4(4):729-39. PMID:7613470

Page seeded by OCA on Thu Feb 21 14:16:07 2008

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OCA

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-[[Image:1ocp.gif|left|200px]]<br /><applet load="1ocp" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="1ocp" />
 '''SOLUTION STRUCTURE OF OCT3 POU-HOMEODOMAIN'''<br />
 ==Overview==
-The POU-homeodomain (POUH) forms the bipartite DNA-binding POU domain in, association with the POU-specific domain. The 1H, 15N, and 13C magnetic, resonances of the 67-amino acid long POUH of mouse Oct-3 have almost, completely been assigned, mainly through the combined use of, three-dimensional triple resonance NMR methods. Based on the distance and, dihedral angle constraints derived from the NMR data, the solution, structure of the POUH domain has been calculated by the ab initio, simulated annealing method. The average RMS deviation for all backbone, heavy atoms of the 20 best calculated structures for residues 9-53 of the, total 67 amino acid residues is 0.44 A. The POUH domain consists of three, alpha-helices (helix-I, 10-20; helix-II, 28-38; and helix-III, 42-53), and, helices-II and -III form a helix-turn-helix motif. In comparison with, other classical homeodomains, the folding of the three helices is quite, similar. However, the length of helix-III is fairly short. In the complex, of the Oct-1 POU domain with an octamer site (Klemm JD, et al., 1994, Cell, 77:21-32), the corresponding region is involved in helix-III. The, structural difference between these two cases will be discussed.
+The POU-homeodomain (POUH) forms the bipartite DNA-binding POU domain in association with the POU-specific domain. The 1H, 15N, and 13C magnetic resonances of the 67-amino acid long POUH of mouse Oct-3 have almost completely been assigned, mainly through the combined use of three-dimensional triple resonance NMR methods. Based on the distance and dihedral angle constraints derived from the NMR data, the solution structure of the POUH domain has been calculated by the ab initio simulated annealing method. The average RMS deviation for all backbone heavy atoms of the 20 best calculated structures for residues 9-53 of the total 67 amino acid residues is 0.44 A. The POUH domain consists of three alpha-helices (helix-I, 10-20; helix-II, 28-38; and helix-III, 42-53), and helices-II and -III form a helix-turn-helix motif. In comparison with other classical homeodomains, the folding of the three helices is quite similar. However, the length of helix-III is fairly short. In the complex of the Oct-1 POU domain with an octamer site (Klemm JD, et al., 1994, Cell 77:21-32), the corresponding region is involved in helix-III. The structural difference between these two cases will be discussed.
 ==About this Structure==
-OCP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OCP OCA].
+OCP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OCP OCA].
 ==Reference==
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 [[Category: Hayashi, F.]]
 [[Category: Kyogoku, Y.]]
-[[Category: Morita, E.H.]]
+[[Category: Morita, E H.]]
 [[Category: Shirakawa, M.]]
 [[Category: dna-binding protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:54:56 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:16:07 2008''