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1lto

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[[Image:1lto.gif|left|200px]]
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{{Structure
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Tryptase Tryptase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.59 3.4.21.59] </span>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lto FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lto OCA], [http://www.ebi.ac.uk/pdbsum/1lto PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lto RCSB]</span>
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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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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:16:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:07:13 2008''
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Revision as of 21:16, 2 May 2008

Image:1lto.gif

Template:STRUCTURE 1lto

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

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