1lto: Difference between revisions

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-[[Image:1lto.gif|left|200px]]
- {{Structure
+==Human alpha1-tryptase==
-|PDB= 1lto |SIZE=350|CAPTION= <scene name='initialview01'>1lto</scene>, resolution 2.20&Aring;
+<StructureSection load='1lto' size='340' side='right'caption='[[1lto]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND=
+<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>
-|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]
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
-|GENE=
+<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>
+== 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 ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lt/1lto_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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="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.
-'''Human alpha1-tryptase'''
+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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1lto" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-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.
+*[[Tryptase|Tryptase]]
+== References ==
-==About this Structure==
+<references/>
-LTO 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].
+__TOC__
+</StructureSection>
-==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://www.ncbi.nlm.nih.gov/pubmed/12162961 12162961]
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Tryptase]]
+[[Category: Bode W]]
-[[Category: Bode, W.]]
+[[Category: Huber R]]
-[[Category: Huber, R.]]
+[[Category: Marquardt U]]
-[[Category: Marquardt, U.]]
+[[Category: Sommerhoff CP]]
-[[Category: Sommerhoff, C P.]]
+[[Category: Zettl F]]
-[[Category: Zettl, F.]]
-[[Category: hydrolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:35:03 2008''