1h2w: Difference between revisions

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Revision as of 22:13, 14 March 2011

File:1h2w.png

Template:STRUCTURE 1h2w

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAINPROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN

Template:ABSTRACT PUBMED 12202494

About this StructureAbout this Structure

1h2w is a 1 chain structure. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1][xtra 2][xtra 3][xtra 4]

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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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OCA
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