1a0l: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1a0l]] 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=1A0L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A0L FirstGlance]. <br>
<table><tr><td colspan='2'>[[1a0l]] 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=1A0L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A0L FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APA:(2S)-3-(4-CARBAMIMIDOYLPHENYL)-2-HYDROXYPROPANOIC+ACID'>APA</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Tryptase Tryptase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.59 3.4.21.59] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APA:(2S)-3-(4-CARBAMIMIDOYLPHENYL)-2-HYDROXYPROPANOIC+ACID'>APA</scene></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=1a0l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a0l OCA], [https://pdbe.org/1a0l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a0l RCSB], [https://www.ebi.ac.uk/pdbsum/1a0l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a0l 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=1a0l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a0l OCA], [https://pdbe.org/1a0l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a0l RCSB], [https://www.ebi.ac.uk/pdbsum/1a0l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a0l ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/TRYB2_HUMAN TRYB2_HUMAN]] Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. Has an immunoprotective role during bacterial infection. Required to efficiently combat K.pneumoniae infection (By similarity).  
[https://www.uniprot.org/uniprot/TRYB2_HUMAN TRYB2_HUMAN] Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. Has an immunoprotective role during bacterial infection. Required to efficiently combat K.pneumoniae infection (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=1a0l 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=1a0l ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human tryptase, a mast-cell-specific serine proteinase that may be involved in causing asthma and other allergic and inflammatory disorders, is unique in two respects: it is enzymatically active only as a heparin-stabilized tetramer, and it is resistant to all known endogenous proteinase inhibitors. The 3-A crystal structure of human beta-tryptase in a complex with 4-amidinophenyl pyruvic acid shows four quasi-equivalent monomers arranged in a square flat ring of pseudo 222 symmetry. Each monomer contacts its neighbours at two different interfaces through six loop segments. These loops are located around the active site of beta-tryptase and differ considerably in length and conformation from loops of other trypsin-like proteinases. The four active centres of the tetramer are directed towards an oval central pore, restricting access for macromolecular substrates and enzyme inhibitors. Heparin chains might stabilize the complex by binding to an elongated patch of positively charged residues spanning two adjacent monomers. The nature of this unique tetrameric architecture explains many of tryptase's biochemical properties and provides a basis for the rational design of monofunctional and bifunctional tryptase inhibitors.
Human beta-tryptase is a ring-like tetramer with active sites facing a central pore.,Pereira PJ, Bergner A, Macedo-Ribeiro S, Huber R, Matschiner G, Fritz H, Sommerhoff CP, Bode W Nature. 1998 Mar 19;392(6673):306-11. PMID:9521329<ref>PMID:9521329</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1a0l" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Tryptase|Tryptase]]
*[[Tryptase|Tryptase]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Tryptase]]
[[Category: Bergner A]]
[[Category: Bergner, A]]
[[Category: Bode W]]
[[Category: Bode, W]]
[[Category: Fritz H]]
[[Category: Fritz, H]]
[[Category: Huber R]]
[[Category: Huber, R]]
[[Category: Macedo-Ribeiro S]]
[[Category: Macedo-Ribeiro, S]]
[[Category: Matschiner G]]
[[Category: Matschiner, G]]
[[Category: Pereira PJB]]
[[Category: Pereira, P J.B]]
[[Category: Sommerhoff CP]]
[[Category: Sommerhoff, C P]]
[[Category: Allergy]]
[[Category: Asthma]]
[[Category: Heparin]]
[[Category: Hydrolase-hydrolase inhibitor complex]]
[[Category: Serine proteinase]]
[[Category: Tetramer]]
[[Category: Trypsin-like serine proteinase]]
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