1lto: Difference between revisions

Revision as of 22:12, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1lto.png

Template:STRUCTURE 1lto

Human alpha1-tryptaseHuman alpha1-tryptase

Template:ABSTRACT PUBMED 12162961

About this StructureAbout this Structure

1LTO is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

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 Wed Jul 2 22:12:17 2008

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OCA

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-'''Human alpha1-tryptase'''
+===Human alpha1-tryptase===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12162961}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_12162961}}
 ==About this Structure==
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 [[Category: Zettl, F.]]
 [[Category: Hydrolase]]
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