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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: Journal Article
Alternative Title : J. Mol. Biol.

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 Creators:
Marquardt, U.1, Author              
Zettl, F., Author
Huber, R.1, Author              
Bode, W.1, 2, 3, Author              
Sommerhoff, C. P., Author
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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Free keywords: tryptase; asthma; mast cells; allergy; X-ray crystallography
 Abstract: 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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Language(s): eng - English
 Dates: 2002-08-16
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 41684
ISI: 000177761300009
 Degree: -

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Title: Journal of Molecular Biology
  Alternative Title : J. Mol. Biol.
Source Genre: Journal
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Pages: - Volume / Issue: 321 (3) Sequence Number: - Start / End Page: 491 - 502 Identifier: ISSN: 0022-2836