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1kbn
From Proteopedia
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{{STRUCTURE_1kbn| PDB=1kbn | SCENE= }} | {{STRUCTURE_1kbn| PDB=1kbn | SCENE= }} | ||
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===Glutathione transferase mutant=== | ===Glutathione transferase mutant=== | ||
| + | ==Function== | ||
| + | [[http://www.uniprot.org/uniprot/GSTP1_HUMAN GSTP1_HUMAN]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration.<ref>PMID:21668448</ref> | ||
==About this Structure== | ==About this Structure== | ||
[[1kbn]] is a 2 chain structure with 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=1KBN OCA]. | [[1kbn]] is a 2 chain structure with 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=1KBN OCA]. | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Glutathione S-transferase|Glutathione S-transferase]] | ||
| + | |||
| + | ==Reference== | ||
| + | <references group="xtra"/><references/> | ||
[[Category: Glutathione transferase]] | [[Category: Glutathione transferase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
Revision as of 10:34, 16 April 2014
Contents |
Glutathione transferase mutant
Function
[GSTP1_HUMAN] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration.[1]
About this Structure
1kbn is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- ↑ Sun KH, Chang KH, Clawson S, Ghosh S, Mirzaei H, Regnier F, Shah K. Glutathione-S-transferase P1 is a critical regulator of Cdk5 kinase activity. J Neurochem. 2011 Sep;118(5):902-14. doi: 10.1111/j.1471-4159.2011.07343.x. Epub , 2011 Jul 8. PMID:21668448 doi:10.1111/j.1471-4159.2011.07343.x
