1lto
From Proteopedia
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| - | [[Image:1lto.gif|left|200px]] | + | [[Image:1lto.gif|left|200px]] |
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| - | '''Human alpha1-tryptase''' | + | {{Structure |
| + | |PDB= 1lto |SIZE=350|CAPTION= <scene name='initialview01'>1lto</scene>, resolution 2.20Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Human alpha1-tryptase''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LTO is a [ | + | 1LTO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LTO OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12162961 12162961] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:35:03 2008'' |
Revision as of 10:35, 20 March 2008
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| , resolution 2.20Å | |||||||
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| Activity: | Tryptase, with EC number 3.4.21.59 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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