1cvr

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[[Image:1cvr.gif|left|200px]]
[[Image:1cvr.gif|left|200px]]
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{{Structure
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|PDB= 1cvr |SIZE=350|CAPTION= <scene name='initialview01'>1cvr</scene>, resolution 2.0&Aring;
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The line below this paragraph, containing "STRUCTURE_1cvr", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ACL:DEOXY-CHLOROMETHYL-ARGININE'>ACL</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DPN:D-PHENYLALANINE'>DPN</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Gingipain_R Gingipain R], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.37 3.4.22.37] </span>
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{{STRUCTURE_1cvr| PDB=1cvr | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cvr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cvr OCA], [http://www.ebi.ac.uk/pdbsum/1cvr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cvr RCSB]</span>
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}}
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'''CRYSTAL STRUCTURE OF THE ARG SPECIFIC CYSTEINE PROTEINASE GINGIPAIN R (RGPB)'''
'''CRYSTAL STRUCTURE OF THE ARG SPECIFIC CYSTEINE PROTEINASE GINGIPAIN R (RGPB)'''
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[[Category: Beisel, H G.]]
[[Category: Beisel, H G.]]
[[Category: Eichinger, A.]]
[[Category: Eichinger, A.]]
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[[Category: caspase]]
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[[Category: Caspase]]
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[[Category: cysteine proteinase]]
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[[Category: Cysteine proteinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:09:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:29:35 2008''
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Revision as of 10:09, 2 May 2008

Template:STRUCTURE 1cvr

CRYSTAL STRUCTURE OF THE ARG SPECIFIC CYSTEINE PROTEINASE GINGIPAIN R (RGPB)


Overview

Gingipains are cysteine proteinases acting as key virulence factors of the bacterium Porphyromonas gingivalis, the major pathogen in periodontal disease. The 1.5 and 2.0 A crystal structures of free and D-Phe-Phe-Arg-chloromethylketone-inhibited gingipain R reveal a 435-residue, single-polypeptide chain organized into a catalytic and an immunoglobulin-like domain. The catalytic domain is subdivided into two subdomains comprising four- and six-stranded beta-sheets sandwiched by alpha-helices. Each subdomain bears topological similarities to the p20-p10 heterodimer of caspase-1. The second subdomain harbours the Cys-His catalytic diad and a nearby Glu arranged around the S1 specificity pocket, which carries an Asp residue to enforce preference for Arg-P1 residues. This gingipain R structure is an excellent template for the rational design of drugs with a potential to cure and prevent periodontitis. Here we show the binding mode of an arginine-containing inhibitor in the active-site, thus identifying major interaction sites defining a suitable pharmacophor.

About this Structure

1CVR is a Single protein structure of sequence from Porphyromonas gingivalis. Full crystallographic information is available from OCA.

Reference

Crystal structure of gingipain R: an Arg-specific bacterial cysteine proteinase with a caspase-like fold., Eichinger A, Beisel HG, Jacob U, Huber R, Medrano FJ, Banbula A, Potempa J, Travis J, Bode W, EMBO J. 1999 Oct 15;18(20):5453-62. PMID:10523290 Page seeded by OCA on Fri May 2 13:09:46 2008

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