1h2x: Difference between revisions

Revision as of 22:39, 14 March 2011

1h2x is a 1 chain structure. Full crystallographic information is available from OCA.

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:https://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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-{{Seed}}
 [[Image:1h2x.png|left|200px]]
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 ==About this Structure==
-H2X is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H2X OCA].
+[[1h2x]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H2X OCA].
 ==Reference==
-<ref group="xtra">PMID:12202494</ref><references group="xtra"/>
+<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"/>
 [[Category: Prolyl oligopeptidase]]
 [[Category: Fulop, V.]]
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 [[Category: Prolyl oligopeptidase]]
 [[Category: Serine protease]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 09:29:32 2009''