1vz2

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[[Image:1vz2.png|left|200px]]
[[Image:1vz2.png|left|200px]]
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{{STRUCTURE_1vz2| PDB=1vz2 | SCENE= }}
{{STRUCTURE_1vz2| PDB=1vz2 | SCENE= }}
===PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, Y73C/V427C/C255T MUTANT===
===PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, Y73C/V427C/C255T MUTANT===
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{{ABSTRACT_PUBMED_15210359}}
{{ABSTRACT_PUBMED_15210359}}
==About this Structure==
==About this Structure==
[[1vz2]] 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=1VZ2 OCA].
[[1vz2]] 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=1VZ2 OCA].
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==See Also==
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*[[Prolyl Endopeptidase|Prolyl Endopeptidase]]
==Reference==
==Reference==
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<ref group="xtra">PMID:15210359</ref><ref group="xtra">PMID:14514675</ref><ref group="xtra">PMID:12202494</ref><ref group="xtra">PMID:12228249</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:015210359</ref><ref group="xtra">PMID:014514675</ref><ref group="xtra">PMID:012202494</ref><ref group="xtra">PMID:012228249</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]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]

Revision as of 12:34, 23 January 2013

Image:1vz2.png

Template:STRUCTURE 1vz2

Contents

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, Y73C/V427C/C255T MUTANT

Template:ABSTRACT PUBMED 15210359

About this Structure

1vz2 is a 1 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA.

See Also

Reference

  • Szeltner Z, Rea D, Juhasz T, Renner V, Fulop V, Polgar L. Concerted structural changes in the peptidase and the propeller domains of prolyl oligopeptidase are required for substrate binding. J Mol Biol. 2004 Jul 9;340(3):627-37. PMID:15210359 doi:10.1016/j.jmb.2004.05.011
  • Szeltner Z, Rea D, Renner V, Juliano L, Fulop V, Polgar L. Electrostatic environment at the active site of prolyl oligopeptidase is highly influential during substrate binding. J Biol Chem. 2003 Dec 5;278(49):48786-93. Epub 2003 Sep 25. PMID:14514675 doi:10.1074/jbc.M309555200
  • 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
  • Szeltner Z, Rea D, Juhasz T, Renner V, Mucsi Z, Orosz G, Fulop V, Polgar L. Substrate-dependent competency of the catalytic triad of prolyl oligopeptidase. J Biol Chem. 2002 Nov 22;277(47):44597-605. Epub 2002 Sep 11. PMID:12228249 doi:http://dx.doi.org/10.1074/jbc.M207386200
  • 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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