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1a0l

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[[Image:1a0l.gif|left|200px]]
 
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{{Structure
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==HUMAN BETA-TRYPTASE: A RING-LIKE TETRAMER WITH ACTIVE SITES FACING A CENTRAL PORE==
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|PDB= 1a0l |SIZE=350|CAPTION= <scene name='initialview01'>1a0l</scene>, resolution 3.0&Aring;
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<StructureSection load='1a0l' size='340' side='right'caption='[[1a0l]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=APA:AMIDO+PHENYL+PYRUVIC+ACID'>APA</scene>
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<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>
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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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</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>
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|GENE=
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<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>
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|DOMAIN=
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<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>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a0l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a0l OCA], [http://www.ebi.ac.uk/pdbsum/1a0l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a0l RCSB]</span>
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== Function ==
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}}
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[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).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a0/1a0l_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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].
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<div style="clear:both"></div>
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'''HUMAN BETA-TRYPTASE: A RING-LIKE TETRAMER WITH ACTIVE SITES FACING A CENTRAL PORE'''
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==See Also==
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*[[Tryptase|Tryptase]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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==About this Structure==
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1A0L 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=1A0L OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/9521329 9521329]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Tryptase]]
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[[Category: Bergner A]]
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[[Category: Bergner, A.]]
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[[Category: Bode W]]
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[[Category: Bode, W.]]
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[[Category: Fritz H]]
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[[Category: Fritz, H.]]
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[[Category: Huber R]]
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[[Category: Huber, R.]]
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[[Category: Macedo-Ribeiro S]]
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[[Category: Macedo-Ribeiro, S.]]
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[[Category: Matschiner G]]
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[[Category: Matschiner, G.]]
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[[Category: Pereira PJB]]
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[[Category: Pereira, P J.B.]]
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[[Category: Sommerhoff CP]]
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[[Category: Sommerhoff, C P.]]
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[[Category: allergy]]
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[[Category: asthma]]
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[[Category: heparin]]
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[[Category: tetramer]]
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[[Category: trypsin-like serine proteinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:30:34 2008''
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Current revision

HUMAN BETA-TRYPTASE: A RING-LIKE TETRAMER WITH ACTIVE SITES FACING A CENTRAL PORE

PDB ID 1a0l

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