3grs: Difference between revisions
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[[Image:3grs.png|left|200px]] | [[Image:3grs.png|left|200px]] | ||
{{STRUCTURE_3grs| PDB=3grs | SCENE= }} | {{STRUCTURE_3grs| PDB=3grs | SCENE= }} | ||
===REFINED STRUCTURE OF GLUTATHIONE REDUCTASE AT 1.54 ANGSTROMS RESOLUTION=== | ===REFINED STRUCTURE OF GLUTATHIONE REDUCTASE AT 1.54 ANGSTROMS RESOLUTION=== | ||
{{ABSTRACT_PUBMED_3656429}} | {{ABSTRACT_PUBMED_3656429}} | ||
==About this Structure== | ==About this Structure== | ||
[[3grs]] is a 1 chain structure of [[Glutathione Reductase]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entries and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1grs 1grs]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GRS OCA]. | |||
==See Also== | |||
*[[Glutathione Reductase|Glutathione Reductase]] | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:003656429</ref><ref group="xtra">PMID:009174360</ref><ref group="xtra">PMID:009546215</ref><ref group="xtra">PMID:011917145</ref><ref group="xtra">PMID:012215419</ref><references group="xtra"/> | ||
[[Category: Glutathione-disulfide reductase]] | [[Category: Glutathione-disulfide reductase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Karplus, P A.]] | [[Category: Karplus, P A.]] | ||
[[Category: Schulz, G E.]] | [[Category: Schulz, G E.]] | ||
Revision as of 16:51, 25 July 2012
REFINED STRUCTURE OF GLUTATHIONE REDUCTASE AT 1.54 ANGSTROMS RESOLUTIONREFINED STRUCTURE OF GLUTATHIONE REDUCTASE AT 1.54 ANGSTROMS RESOLUTION
Template:ABSTRACT PUBMED 3656429
About this StructureAbout this Structure
3grs is a 1 chain structure of Glutathione Reductase with sequence from Homo sapiens. This structure supersedes the now removed PDB entries and 1grs. Full crystallographic information is available from OCA.
See AlsoSee Also
ReferenceReference
[xtra 1][xtra 2][xtra 3][xtra 4][xtra 5]
- ↑ Karplus PA, Schulz GE. Refined structure of glutathione reductase at 1.54 A resolution. J Mol Biol. 1987 Jun 5;195(3):701-29. PMID:3656429
- ↑ Stoll VS, Simpson SJ, Krauth-Siegel RL, Walsh CT, Pai EF. Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity. Biochemistry. 1997 May 27;36(21):6437-47. PMID:9174360 doi:10.1021/bi963074p
- ↑ Becker K, Savvides SN, Keese M, Schirmer RH, Karplus PA. Enzyme inactivation through sulfhydryl oxidation by physiologic NO-carriers. Nat Struct Biol. 1998 Apr;5(4):267-71. PMID:9546215
- ↑ Bhattacharyya R, Samanta U, Chakrabarti P. Aromatic-aromatic interactions in and around alpha-helices. Protein Eng. 2002 Feb;15(2):91-100. PMID:11917145
- ↑ Ermolenko DN, Thomas ST, Aurora R, Gronenborn AM, Makhatadze GI. Hydrophobic interactions at the Ccap position of the C-capping motif of alpha-helices. J Mol Biol. 2002 Sep 6;322(1):123-35. PMID:12215419