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==human beta-tryptase II complexed with 4-piperidinebutyrate to make acylenzyme== | ==human beta-tryptase II complexed with 4-piperidinebutyrate to make acylenzyme== | ||
<StructureSection load='2fww' size='340' side='right' caption='[[2fww]], [[Resolution|resolution]] 2.25Å' scene=''> | <StructureSection load='2fww' size='340' side='right'caption='[[2fww]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2fww]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2fww]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FWW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FWW FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C1R:4-PIPERIDINEBUTYRATE'>C1R</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C1R:4-PIPERIDINEBUTYRATE'>C1R</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2fx4|2fx4]], [[2fx6|2fx6]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2fx4|2fx4]], [[2fx6|2fx6]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TPSB2, TPS2 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TPSB2, TPS2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fww OCA], [https://pdbe.org/2fww PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fww RCSB], [https://www.ebi.ac.uk/pdbsum/2fww PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fww 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). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fw/2fww_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fw/2fww_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
| Line 31: | Line 31: | ||
</div> | </div> | ||
<div class="pdbe-citations 2fww" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2fww" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Tryptase|Tryptase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 36: | Line 39: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Tryptase]] | [[Category: Tryptase]] | ||
[[Category: Katz, B A]] | [[Category: Katz, B A]] | ||
Latest revision as of 18:35, 3 March 2021
human beta-tryptase II complexed with 4-piperidinebutyrate to make acylenzymehuman beta-tryptase II complexed with 4-piperidinebutyrate to make acylenzyme
Structural highlights
Function[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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedImproved peptide-based inhibitors of human beta tryptase were discovered using information gleaned from tripeptide library screening and structure-guided design methods, including fragment screening. Our efforts sought to improve this class of inhibitors by replacing the traditional Lys or Arg P1 element. The optimized compounds display low nanomolar potency against the mast cell target and several hundred-fold selectivity with respect to serine protease off targets. Thus, replacement of Lys/Arg at P1 in a peptide-like scaffold does not need to be accompanied by a loss in target affinity. Structure-guided design of peptide-based tryptase inhibitors.,McGrath ME, Sprengeler PA, Hirschbein B, Somoza JR, Lehoux I, Janc JW, Gjerstad E, Graupe M, Estiarte A, Venkataramani C, Liu Y, Yee R, Ho JD, Green MJ, Lee CS, Liu L, Tai V, Spencer J, Sperandio D, Katz BA Biochemistry. 2006 May 16;45(19):5964-73. PMID:16681368[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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