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Titolo:
Crystal structure of gingipain R: an Arg-specific bacterial cysteine proteinase with a caspase-like fold
Autore:
Eichinger, A; Beisel, HG; Jacob, U; Huber, R; Medrano, FJ; Banbula, A; Potempa, J; Travis, J; Bode, W;
Indirizzi:
Max Planck Inst Biochem, Abt Strukturforsch, D-82152 Martinsried, Germany Max Planck Inst Biochem Martinsried Germany D-82152 Martinsried, Germany CSIC, Ctr Invest Biol, Dept Microbiol, E-28006 Madrid, Spain CSIC MadridSpain E-28006 st Biol, Dept Microbiol, E-28006 Madrid, Spain Jagiellonian Univ, Inst Mol Biol, PL-31120 Krakow, Poland Jagiellonian Univ Krakow Poland PL-31120 l Biol, PL-31120 Krakow, Poland Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA Univ Georgia Athens GA USA 30602 Biochem & Mol Biol, Athens, GA 30602 USA
Titolo Testata:
EMBO JOURNAL
fascicolo: 20, volume: 18, anno: 1999,
pagine: 5453 - 5462
SICI:
0261-4189(19991015)18:20<5453:CSOGRA>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
INTERLEUKIN-1-BETA CONVERTING-ENZYME; PORPHYROMONAS-GINGIVALIS; MOLECULAR-CLONING; ACTIVE-SITE; ARGININE; PROTEASE; GENES; PERIODONTITIS; REFINEMENT; PROGRAM;
Keywords:
caspases; crystal structure; cysteine proteinase; periodontitis; Porphyromonas gingivalis;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
54
Recensione:
Indirizzi per estratti:
Indirizzo: Bode, W Max Planck Inst Biochem, Abt Strukturforsch, D-82152 Martinsried, Germany Max Planck Inst Biochem Martinsried Germany D-82152 ied, Germany
Citazione:
A. Eichinger et al., "Crystal structure of gingipain R: an Arg-specific bacterial cysteine proteinase with a caspase-like fold", EMBO J, 18(20), 1999, pp. 5453-5462

Abstract

Gingipains are cysteine proteinases acting as key virulence factors of thebacterium Porphyromonas gingivalis, the major pathogen in periodontal disease. The 1.5 and 2.0 Angstrom 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- andsix-stranded beta-sheets sandwiched by alpha-helices, Each subdomain bearstopological 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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 22/09/20 alle ore 06:23:54