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

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons78361

Marquardt,  U.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78142

Huber,  R.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons77772

Bode,  W.
Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society;
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Zitation

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.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0010-6E7C-9
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.