1uoq
From Proteopedia
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[[Image:1uoq.png|left|200px]] | [[Image:1uoq.png|left|200px]] | ||
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===PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, S554A MUTANT WITH BOUND PEPTIDE LIGAND GLU-PHE-SER-PRO=== | ===PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, S554A MUTANT WITH BOUND PEPTIDE LIGAND GLU-PHE-SER-PRO=== | ||
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{{ABSTRACT_PUBMED_14514675}} | {{ABSTRACT_PUBMED_14514675}} | ||
==About this Structure== | ==About this Structure== | ||
[[1uoq]] is a 2 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=1UOQ OCA]. | [[1uoq]] is a 2 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=1UOQ OCA]. | ||
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| + | ==See Also== | ||
| + | *[[Prolyl Endopeptidase|Prolyl Endopeptidase]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <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 09:36, 16 January 2013
Contents |
PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, S554A MUTANT WITH BOUND PEPTIDE LIGAND GLU-PHE-SER-PRO
Template:ABSTRACT PUBMED 14514675
About this Structure
1uoq is a 2 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA.
See Also
Reference
- 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
