1lto
From Proteopedia
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[[Image:1lto.gif|left|200px]] | [[Image:1lto.gif|left|200px]] | ||
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'''Human alpha1-tryptase''' | '''Human alpha1-tryptase''' | ||
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[[Category: Sommerhoff, C P.]] | [[Category: Sommerhoff, C P.]] | ||
[[Category: Zettl, F.]] | [[Category: Zettl, F.]] | ||
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Revision as of 21:16, 2 May 2008
Human alpha1-tryptase
Overview
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 2.2A 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.
About this Structure
1LTO is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The crystal structure of human alpha1-tryptase reveals a blocked substrate-binding region., Marquardt U, Zettl F, Huber R, Bode W, Sommerhoff C, J Mol Biol. 2002 Aug 16;321(3):491-502. PMID:12162961 Page seeded by OCA on Sat May 3 00:16:38 2008