1h2y

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[[Image:1h2y.png|left|200px]]
 
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{{STRUCTURE_1h2y| PDB=1h2y | SCENE= }}
{{STRUCTURE_1h2y| PDB=1h2y | SCENE= }}
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===PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, Y473F MUTANT WITH COVALENTLY BOUND INHIBITOR Z-PRO-PROLINAL===
===PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, Y473F MUTANT WITH COVALENTLY BOUND INHIBITOR Z-PRO-PROLINAL===
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{{ABSTRACT_PUBMED_12202494}}
{{ABSTRACT_PUBMED_12202494}}

Revision as of 09:55, 11 March 2013

Template:STRUCTURE 1h2y

Contents

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, Y473F MUTANT WITH COVALENTLY BOUND INHIBITOR Z-PRO-PROLINAL

Template:ABSTRACT PUBMED 12202494

About this Structure

1h2y is a 1 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA.

See Also

Reference

  • Szeltner Z, Rea D, Renner V, Fulop V, Polgar L. Electrostatic effects and binding determinants in the catalysis of prolyl oligopeptidase. Site specific mutagenesis at the oxyanion binding site. J Biol Chem. 2002 Nov 8;277(45):42613-22. Epub 2002 Aug 28. PMID:12202494 doi:10.1074/jbc.M208043200
  • Fulop V, Szeltner Z, Renner V, Polgar L. Structures of prolyl oligopeptidase substrate/inhibitor complexes. Use of inhibitor binding for titration of the catalytic histidine residue. J Biol Chem. 2001 Jan 12;276(2):1262-6. PMID:11031266 doi:http://dx.doi.org/10.1074/jbc.M007003200
  • Fulop V, Szeltner Z, Polgar L. Catalysis of serine oligopeptidases is controlled by a gating filter mechanism. EMBO Rep. 2000 Sep;1(3):277-81. PMID:11256612 doi:10.1093/embo-reports/kvd048
  • Fulop V, Bocskei Z, Polgar L. Prolyl oligopeptidase: an unusual beta-propeller domain regulates proteolysis. Cell. 1998 Jul 24;94(2):161-70. PMID:9695945

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