1gss: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gss OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gss RCSB], [http://www.ebi.ac.uk/pdbsum/1gss PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gss OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gss RCSB], [http://www.ebi.ac.uk/pdbsum/1gss PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== 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> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 21:31, 24 December 2014
THREE-DIMENSIONAL STRUCTURE OF CLASS PI GLUTATHIONE S-TRANSFERASE FROM HUMAN PLACENTA IN COMPLEX WITH S-HEXYLGLUTATHIONE AT 2.8 ANGSTROMS RESOLUTIONTHREE-DIMENSIONAL STRUCTURE OF CLASS PI GLUTATHIONE S-TRANSFERASE FROM HUMAN PLACENTA IN COMPLEX WITH S-HEXYLGLUTATHIONE AT 2.8 ANGSTROMS RESOLUTION
Structural highlights
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] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe three-dimensional structure of human class pi glutathione S-transferase from placenta (hGSTP1-1), a homodimeric enzyme, has been solved by Patterson search methods and refined at 2.8 A resolution to a final crystallographic R-factor of 19.6% (8.0 to 2.8 A resolution). Subunit folding topology, subunit overall structure and subunit association closely resembles the structure of porcine class pi glutathione S-transferase. The binding site of a competitive inhibitor, S-hexylglutathione, is analyzed and the locations of the binding regions for glutathione (G-site) and electrophilic substrates (H-site) are determined. The specific interactions between protein and the inhibitor's glutathione peptide are the same as those observed between glutathione sulfonate and the porcine isozyme. The H-site is located adjacent to the G-site, with the hexyl moiety lying above a segment (residues 8 to 10) connecting strand beta 1 and helix alpha A where it is in hydrophobic contact with Tyr7, Phe8, Val10, Val35 and Tyr106. Catalytic models are discussed on the basis of the molecular structure. Three-dimensional structure of class pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 A resolution.,Reinemer P, Dirr HW, Ladenstein R, Huber R, Lo Bello M, Federici G, Parker MW J Mol Biol. 1992 Sep 5;227(1):214-26. PMID:1522586[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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