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1h2z

From Proteopedia

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==About this Structure==
==About this Structure==
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[[1h2z]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H2Z OCA].
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[[1h2z]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H2Z OCA].
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==See Also==
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*[[Prolyl Endopeptidase]]
==Reference==
==Reference==
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<ref group="xtra">PMID:12202494</ref><ref group="xtra">PMID:11031266</ref><ref group="xtra">PMID:11256612</ref><ref group="xtra">PMID:9695945</ref><references group="xtra"/>
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<ref group="xtra">PMID:012202494</ref><ref group="xtra">PMID:011031266</ref><ref group="xtra">PMID:011256612</ref><ref group="xtra">PMID:009695945</ref><references group="xtra"/>
[[Category: Prolyl oligopeptidase]]
[[Category: Prolyl oligopeptidase]]
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[[Category: Sus scrofa]]
[[Category: Fulop, V.]]
[[Category: Fulop, V.]]
[[Category: Rea, D.]]
[[Category: Rea, D.]]

Revision as of 06:17, 24 August 2011

Image:1h2z.png

Template:STRUCTURE 1h2z

Contents

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, S554A MUTANT WITH BOUND PEPTIDE LIGAND SUC-GLY-PRO

Template:ABSTRACT PUBMED 12202494

About this Structure

1h2z 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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