1jhb: Difference between revisions

Revision as of 20:14, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1jhb.png

Template:STRUCTURE 1jhb

HUMAN GLUTAREDOXIN IN FULLY REDUCED FORM, NMR, 20 STRUCTURESHUMAN GLUTAREDOXIN IN FULLY REDUCED FORM, NMR, 20 STRUCTURES

Template:ABSTRACT PUBMED 9677297

About this StructureAbout this Structure

1JHB is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

The NMR solution structure of human glutaredoxin in the fully reduced form., Sun C, Berardi MJ, Bushweller JH, J Mol Biol. 1998 Jul 24;280(4):687-701. PMID:9677297

Page seeded by OCA on Tue Jul 1 20:14:41 2008

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

OCA

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-[[Image:1jhb.gif|left|200px]]
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 {{STRUCTURE_1jhb|  PDB=1jhb  |  SCENE=  }}
-'''HUMAN GLUTAREDOXIN IN FULLY REDUCED FORM, NMR, 20 STRUCTURES'''
+===HUMAN GLUTAREDOXIN IN FULLY REDUCED FORM, NMR, 20 STRUCTURES===
-==Overview==
+<!--
-The determination of the nuclear magnetic resonance (NMR) solution structure of fully reduced human glutaredoxin is described. A total of 1159 useful nuclear Overhauser effect (NOE) upper distance constraints and 187 dihedral angle constraints were obtained as the input for the structure calculations for which the torsion angle dynamics program DYANA has been utilized followed by energy minimization in water with the AMBER force field as implemented in the program OPAL. The resulting 20 conformers have an average root-mean-square deviation value relative to the mean coordinates of 0.54 A for all the backbone atoms N, Calpha and C', and of 1.01 A for all heavy atoms. Human glutaredoxin consists of a four-stranded mixed beta-sheet composed of residues 15 to 19, 43 to 47, 72 to 75 and 78 to 81, and five alpha-helices composed of residues 4 to 9, 24 to 34, 54 to 65, 83 to 91, and 94 to 100. Comparisons with the structures of Escherichia coli glutaredoxin-1, pig liver glutaredoxin and human thioredoxin were made. Electrostatic calculations on the human glutaredoxin structure and that of related proteins provide an understanding of the variation of pKa values for the nucleophilic cysteine in the active site observed among these proteins. In addition, the high-resolution NMR solution structure of human glutaredoxin has been used to model the binding site for glutathione and for ribonucleotide reductase B1 by molecular dynamics simulations.
+The line below this paragraph, {{ABSTRACT_PUBMED_9677297}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9677297 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9677297}}
 ==About this Structure==
-JHB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JHB OCA].
+JHB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JHB OCA].
 ==Reference==
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 [[Category: Nmr]]
 [[Category: Oxidoreductase]]
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+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 20:14:41 2008''