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| | <StructureSection load='3u3l' size='340' side='right'caption='[[3u3l]], [[Resolution|resolution]] 1.57Å' scene=''> | | <StructureSection load='3u3l' size='340' side='right'caption='[[3u3l]], [[Resolution|resolution]] 1.57Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3u3l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Horsefly Horsefly]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U3L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U3L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3u3l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tabanus_yao Tabanus yao]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U3L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U3L FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=PR:PRASEODYMIUM+ION'>PR</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]] 1.57Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=PR:PRASEODYMIUM+ION'>PR</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3u3u|3u3u]], [[3u3n|3u3n]]</div></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=3u3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u3l OCA], [https://pdbe.org/3u3l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u3l RCSB], [https://www.ebi.ac.uk/pdbsum/3u3l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u3l 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=3u3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u3l OCA], [https://pdbe.org/3u3l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u3l RCSB], [https://www.ebi.ac.uk/pdbsum/3u3l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u3l ProSAT]</span></td></tr> |
| | </table> | | </table> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Horsefly]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Andersen, J F]] | + | [[Category: Tabanus yao]] |
| - | [[Category: Ribeiro, J M]] | + | [[Category: Andersen JF]] |
| - | [[Category: Xu, X]] | + | [[Category: Ribeiro JM]] |
| - | [[Category: Alphavbeta3 integrin]] | + | [[Category: Xu X]] |
| - | [[Category: Cap domain]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Salivary gland]]
| + | |
| Structural highlights
Publication Abstract from PubMed
The antihemostatic/antiangiogenic protein tablysin-15 is a member of the cysteine-rich secretory, antigen 5 and pathogenesis-related 1 protein (CAP) superfamily and has been shown to bind the integrins alphaIIbbeta3 and alphaVbeta3 by means of an Arg-Gly-Asp (RGD) tripeptide sequence. Here we describe the X-ray crystal structure of tablysin-15 and show that the RGD motif is located in a novel structural context. The motif itself is contained in a type II beta-turn structure that is similar in its conformation to the RGD sequence of the cyclic pentapeptide cilengitide when bound to integrin alphaVbeta3. The CAP domain also contains a hydrophobic channel that appears to bind a fatty acid molecule in the crystal structure after purification from Escherichia coli. After delipidation of the protein, tablysin-15 was found to bind proinflammatory cysteinyl leukotrienes with submicromolar affinities. The structure of the leukotriene E4 (LTE4)-tablysin-15 complex shows that the ligand binds with the non-functionalized end of the fatty acid chain buried in the hydrophobic pocket, while the carboxylate end of the ligand binds forms hydrogen bond/salt bridge interactions with polar side chains at the channel entrance. Therefore, tablysin-15 functions as an inhibitor of integrin function and as an anti-inflammatory scavenger of eicosanoids.
Structure of a protein having inhibitory disintegrin and leukotriene scavenging functions contained in a single domain.,Xu X, Francischetti IM, Lai R, Ribeiro JM, Andersen JF J Biol Chem. 2012 Feb 6. PMID:22311975[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Xu X, Francischetti IM, Lai R, Ribeiro JM, Andersen JF. Structure of a protein having inhibitory disintegrin and leukotriene scavenging functions contained in a single domain. J Biol Chem. 2012 Feb 6. PMID:22311975 doi:10.1074/jbc.M112.340471
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