This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1cvr
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1cvr.gif|left|200px]] | [[Image:1cvr.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1cvr", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{STRUCTURE_1cvr| PDB=1cvr | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''CRYSTAL STRUCTURE OF THE ARG SPECIFIC CYSTEINE PROTEINASE GINGIPAIN R (RGPB)''' | '''CRYSTAL STRUCTURE OF THE ARG SPECIFIC CYSTEINE PROTEINASE GINGIPAIN R (RGPB)''' | ||
| Line 28: | Line 25: | ||
[[Category: Beisel, H G.]] | [[Category: Beisel, H G.]] | ||
[[Category: Eichinger, A.]] | [[Category: Eichinger, A.]] | ||
| - | [[Category: | + | [[Category: Caspase]] |
| - | [[Category: | + | [[Category: Cysteine proteinase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:09:46 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 10:09, 2 May 2008
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
