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  Probing structural determinants distal to the site of hydrolysis that control substrate specificity of the 20S proteasome

Groll, M., Nazif, T., Huber, R., & Bogyo, M. (2002). Probing structural determinants distal to the site of hydrolysis that control substrate specificity of the 20S proteasome. Chemistry & Biology, 9(5), 655-662.

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Genre: Zeitschriftenartikel
Alternativer Titel : Chem. Biol.

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Groll, M.1, Autor           
Nazif, T., Autor
Huber, R.1, Autor           
Bogyo, M., Autor
Affiliations:
1Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565155              

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 Zusammenfassung: The 20S proteasome is a large multicomponent protease complex. Relatively little is known about the mechanisms that control substrate specificity of its multiple active sites. We present here the crystal structure at 2.95 Angstrom resolution of a beta2-selective inhibitor (MB1) bound to the yeast 20S proteasome core particle (CP). This structure is compared to the structure of the CP bound to a general inhibitor (MB2) that covalently modified all three (beta1, beta2, beta5) catalytic subunits. These two inhibitors differ only in their P3 and P4 residues, thereby highlighting binding interactions distal to the active site threonine that control absolute substrate specificity of the complex. Comparisons of the CP-bound structures of MB1, MB2, and the natural products epoxomycin and TMC-95A also provide information regarding general binding modes for several classes of proteasome inhibitors.

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Sprache(n): eng - English
 Datum: 2002-05
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: eDoc: 39344
ISI: 000175777800015
 Art des Abschluß: -

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Titel: Chemistry & Biology
  Alternativer Titel : Chem. Biol.
Genre der Quelle: Zeitschrift
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Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 9 (5) Artikelnummer: - Start- / Endseite: 655 - 662 Identifikator: ISSN: 1074-5521