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3grs
From Proteopedia
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===REFINED STRUCTURE OF GLUTATHIONE REDUCTASE AT 1.54 ANGSTROMS RESOLUTION=== | ===REFINED STRUCTURE OF GLUTATHIONE REDUCTASE AT 1.54 ANGSTROMS RESOLUTION=== | ||
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{{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]. | |
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| + | ==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.]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 13:48:00 2009'' | ||
Revision as of 13:51, 25 July 2012
Contents |
REFINED STRUCTURE OF GLUTATHIONE REDUCTASE AT 1.54 ANGSTROMS RESOLUTION
Template:ABSTRACT PUBMED 3656429
About 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 Also
Reference
- 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
