4q1l

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==Crystal structure of Leucurolysin-a complexed with an endogenous tripeptide (QSW).==
==Crystal structure of Leucurolysin-a complexed with an endogenous tripeptide (QSW).==
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<StructureSection load='4q1l' size='340' side='right' caption='[[4q1l]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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<StructureSection load='4q1l' size='340' side='right'caption='[[4q1l]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4q1l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bothrops_leucurus Bothrops leucurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q1L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q1L FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4q1l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bothrops_leucurus Bothrops leucurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q1L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q1L FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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]] 1.9&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4q1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q1l OCA], [http://pdbe.org/4q1l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4q1l RCSB], [http://www.ebi.ac.uk/pdbsum/4q1l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4q1l ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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=4q1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q1l OCA], [https://pdbe.org/4q1l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q1l RCSB], [https://www.ebi.ac.uk/pdbsum/4q1l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q1l ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/VM1LA_BOTLC VM1LA_BOTLC]] Non-hemorrhagic metalloproteinase that hydrolyzes the alpha chains of fibrinogen, as well as fibrin, fibronectin and casein. Beta and gamma chains are also hydrolyzed, but more slowly. Thrombolytic activity is also observed. Induces detachment of endothelial cells followed by death, and inhibits endothelial cell adhesion to fibronectin. Induces edema in mouse paw. Inhibits ADP-induced platelet aggregation on human platelet-rich plasma with an IC(50) of 2.8 uM.<ref>PMID:16139412</ref> <ref>PMID:17482228</ref>
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[https://www.uniprot.org/uniprot/VM1LA_BOTLC VM1LA_BOTLC] Non-hemorrhagic metalloproteinase that hydrolyzes the alpha chains of fibrinogen, as well as fibrin, fibronectin and casein. Beta and gamma chains are also hydrolyzed, but more slowly. Thrombolytic activity is also observed. Induces detachment of endothelial cells followed by death, and inhibits endothelial cell adhesion to fibronectin. Induces edema in mouse paw. Inhibits ADP-induced platelet aggregation on human platelet-rich plasma with an IC(50) of 2.8 uM.<ref>PMID:16139412</ref> <ref>PMID:17482228</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Leucurolysin-a (leuc-a) is a class P-I snake-venom metalloproteinase isolated from the venom of the South American snake Bothrops leucurus (white-tailed jararaca). The mature protein is composed of 202 amino-acid residues in a single polypeptide chain. It contains a blocked N-terminus and is not glycosylated. In vitro studies revealed that leuc-a dissolves clots made either from purified fibrinogen or from whole blood. Unlike some other venom fibrinolytic metalloproteinases, leuc-a has no haemorrhagic activity. Leuc-a was sequenced and was crystallized using the hanging-drop vapour-diffusion technique. Crystals were obtained using PEG 6000 or PEG 1500. Diffraction data to 1.80 and 1.60 A resolution were collected from two crystals (free enzyme and the endogenous ligand-protein complex, respectively). They both belonged to space group P2(1)2(1)2(1), with very similar unit-cell parameters (a = 44.0, b = 56.2, c = 76.3 A for the free-enzyme crystal).
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Complete amino-acid sequence, crystallization and preliminary X-ray diffraction studies of leucurolysin-a, a nonhaemorrhagic metalloproteinase from Bothrops leucurus snake venom.,Ferreira RN, Rates B, Richardson M, Guimaraes BG, Sanchez EO, Pimenta AM, Nagem RA Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Aug 1;65(Pt 8):798-801., doi: 10.1107/S1744309109025767. Epub 2009 Jul 25. PMID:19652343<ref>PMID:19652343</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4q1l" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Bothrops leucurus]]
[[Category: Bothrops leucurus]]
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[[Category: Ferreira, R N]]
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[[Category: Large Structures]]
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[[Category: Nagem, R A.P]]
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[[Category: Ferreira RN]]
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[[Category: Pimenta, A M.C]]
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[[Category: Nagem RAP]]
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[[Category: Sanchez, E O.F]]
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[[Category: Pimenta AMC]]
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[[Category: Alfa/beta protein]]
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[[Category: Sanchez EOF]]
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[[Category: Hydrolase]]
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[[Category: Metalloendopeptidase]]
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[[Category: Venom compound]]
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[[Category: Zinc binding calcium binding]]
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Current revision

Crystal structure of Leucurolysin-a complexed with an endogenous tripeptide (QSW).

PDB ID 4q1l

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