1vz2: Difference between revisions
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[[Image:1vz2.png|left|200px]] | [[Image:1vz2.png|left|200px]] | ||
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==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]. | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID:15210359</ref><references group="xtra"/> | <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"/> | ||
[[Category: Prolyl oligopeptidase]] | [[Category: Prolyl oligopeptidase]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
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[[Category: Prolyl oligopeptidase]] | [[Category: Prolyl oligopeptidase]] | ||
[[Category: Serine protease]] | [[Category: Serine protease]] | ||
Revision as of 03:37, 15 March 2011
PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, Y73C/V427C/C255T MUTANTPROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, Y73C/V427C/C255T MUTANT
Template:ABSTRACT PUBMED 15210359
About this StructureAbout this Structure
1vz2 is a 1 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA.
ReferenceReference
[xtra 1][xtra 2][xtra 3][xtra 4][xtra 5][xtra 6][xtra 7]
- ↑ 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