1lto
From Proteopedia
(Difference between revisions)
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<StructureSection load='1lto' size='340' side='right'caption='[[1lto]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='1lto' size='340' side='right'caption='[[1lto]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1lto]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1lto]] is a 4 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LTO FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lto FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lto OCA], [https://pdbe.org/1lto PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lto RCSB], [https://www.ebi.ac.uk/pdbsum/1lto PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lto ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lto FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lto OCA], [https://pdbe.org/1lto PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lto RCSB], [https://www.ebi.ac.uk/pdbsum/1lto PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lto ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/TRYB1_HUMAN TRYB1_HUMAN] Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type (By similarity). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lto ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lto ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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. | ||
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| - | 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<ref>PMID:12162961</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1lto" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Tryptase|Tryptase]] | *[[Tryptase|Tryptase]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | + | [[Category: Bode W]] | |
| - | [[Category: Bode | + | [[Category: Huber R]] |
| - | [[Category: Huber | + | [[Category: Marquardt U]] |
| - | [[Category: Marquardt | + | [[Category: Sommerhoff CP]] |
| - | [[Category: Sommerhoff | + | [[Category: Zettl F]] |
| - | [[Category: Zettl | + | |
| - | + | ||
Revision as of 06:06, 3 April 2024
Human alpha1-tryptase
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