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  (R)-3-amidinophenylalanine-derived inhibitors of factor Xa with a novel active-site binding mode

Mueller, M. M., Sperl, S., Stürzebecher, J., Bode, W., & Moroder, L. (2002). (R)-3-amidinophenylalanine-derived inhibitors of factor Xa with a novel active-site binding mode. Biological Chemistry, 383(7-8), 1185-1191.

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Genre: Zeitschriftenartikel
Alternativer Titel : Biol. Chem.

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 Urheber:
Mueller, M. M.1, Autor           
Sperl, S.1, Autor           
Stürzebecher, J.2, Autor           
Bode, W.3, 4, 5, Autor           
Moroder, L.1, Autor           
Affiliations:
1Moroder, Luis / Bioorganic Chemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565160              
2External Organizations, ou_persistent22              
3Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565147              
4Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565155              
5Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              

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Schlagwörter: (R)-3-amidinophenylalanine; factor Xa; novel active-site binding mode; S1 subregion; synthetic inhibitors; X-ray crystal structure
 Zusammenfassung: A putative nonsubstrate like binding mode of (R)-3- amidinophenylalanine derivatives to factor Xa, as derived from modeling experiments based on Xray analysis of their complexes with trypsin, was used to design a new generation of inhibitors. However, the resulting inhibitory potencies were not at all consistent with the working assumption, although with an adamantylureido derivative of (R)-3- amidinophenylalanine phenetyl amide a highly selective nanomolar inhibition of factor Xa was achieved. The Xray analysis of the complex of this ligand with factor Xa revealed an unexpected new binding mode, of which the most important feature is the interaction of the Cterminal aryl moiety with a hydrophobic subregion of the S1 subsite, while the adamantyl group occupies the hydrophobic S3/S4 subsites of the enzyme.

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Sprache(n): eng - English
 Datum: 2002-07
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: eDoc: 35077
ISI: 000177737800021
 Art des Abschluß: -

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Titel: Biological Chemistry
  Alternativer Titel : Biol. Chem.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 383 (7-8) Artikelnummer: - Start- / Endseite: 1185 - 1191 Identifikator: ISSN: 1431-6730