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  The crystal structure of human alpha 1-tryptase reveals a blocked substrate-binding region

Marquardt, U., Zettl, F., Huber, R., Bode, W., & Sommerhoff, C. P. (2002). The crystal structure of human alpha 1-tryptase reveals a blocked substrate-binding region. Journal of Molecular Biology, 321(3), 491-502.

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Genre: Zeitschriftenartikel
Alternativer Titel : J. Mol. Biol.

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 Urheber:
Marquardt, U.1, Autor           
Zettl, F., Autor
Huber, R.1, Autor           
Bode, W.1, 2, 3, Autor           
Sommerhoff, C. P., Autor
Affiliations:
1Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565155              
2Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565147              
3Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              

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Schlagwörter: tryptase; asthma; mast cells; allergy; X-ray crystallography
 Zusammenfassung: Human mast cell tryptases represent a subfamily of trypsin-like serine proteinases implicated in asthma. Unlike beta-tryptases, alpha-tryptases apparently are proteolytically inactive. We have solved the 2.2 Angstrom crystal structure of mature human alpha1-tryptase. It reveals a frame-like tetrameric architecture that, surprisingly, does not require heparin- binding for stability. In marked contrast to beta2-tryptase, the Ser214-Gly219 segment, which normally provides the template for substrate binding, is kinked in alpha-tryptase, thereby blocking its non-primed subsites. This so far unobserved subsite distortion is incompatible with productive substrate binding and processing. alpha-Tryptase apparently is trapped in this off-conformation by repulsions and attractions of the Asp216 side-chain. However, proteolytic activity could be generated by an induced-fit mechanism. (C) 2002 Elsevier Science Ltd. All rights reserved.

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Sprache(n): eng - English
 Datum: 2002-08-16
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: eDoc: 41684
ISI: 000177761300009
 Art des Abschluß: -

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Titel: Journal of Molecular Biology
  Alternativer Titel : J. Mol. Biol.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 321 (3) Artikelnummer: - Start- / Endseite: 491 - 502 Identifikator: ISSN: 0022-2836