1op2: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1op2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Deinagkistrodon_acutus Deinagkistrodon acutus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OP2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OP2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1op2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Deinagkistrodon_acutus Deinagkistrodon acutus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OP2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OP2 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1op0|1op0]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1op0|1op0]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1op2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1op2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1op2 RCSB], [http://www.ebi.ac.uk/pdbsum/1op2 PDBsum]</span></td></tr> | <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=1op2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1op2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1op2 RCSB], [http://www.ebi.ac.uk/pdbsum/1op2 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/VSP2_AGKAC VSP2_AGKAC]] Snake venom serine protease that has fibrinogenolytic activities. Also possess esterolysis and amidolytic activities.<ref>PMID:15632114</ref> <ref>PMID:12595722</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Deinagkistrodon acutus]] | [[Category: Deinagkistrodon acutus]] | ||
[[Category: Niu, L | [[Category: Niu, L]] | ||
[[Category: Teng, M | [[Category: Teng, M]] | ||
[[Category: Zhu, Z | [[Category: Zhu, Z]] | ||
[[Category: Agkistrodon acutus]] | [[Category: Agkistrodon acutus]] | ||
[[Category: Glycoprotein]] | [[Category: Glycoprotein]] | ||
Revision as of 08:46, 25 December 2014
Crystal Structure of AaV-SP-II, a Glycosylated Snake Venom Serine Proteinase from Agkistrodon acutusCrystal Structure of AaV-SP-II, a Glycosylated Snake Venom Serine Proteinase from Agkistrodon acutus
Structural highlights
Function[VSP2_AGKAC] Snake venom serine protease that has fibrinogenolytic activities. Also possess esterolysis and amidolytic activities.[1] [2] 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 PubMedWe deduced that Agkistrodon actus venom serine proteinases I and II, previously isolated from the venom of A. acutus (Zhu, Z., Gong, P., Teng, M., and Niu, L. (2003) Acta Crystallogr. Sect. D Biol. Crystallogr. 59, 547-550), are encoded by two almost identical genes, with only the single substitution Asp for Asn at residue 62. Amidolytic assays indicated that they possess slightly different enzymatic properties. Crystal structures of A. actus venom serine proteinases I and II were determined at resolution of 2.0 and 2.1 A with the identification of trisaccharide (NAG(301)-FUC(302)-NAG(303)) and monosaccharide (NAG(301)) residues in them, respectively. The substrate binding sites S3 of the two proteinases appear much shallower than that of Trimeresurus stejnegeri venom plasminogen activator despite the overall structural similarity. Based on structural analysis, we showed that these Asn(35)-linked oligosaccharides collide spatially with some inhibitors, such as soybean trypsin inhibitor, and would therefore hinder their inhibitory binding. Difference of the carbohydrates in both the proteinases might also lead to their altered catalytic activities. Crystal structures and amidolytic activities of two glycosylated snake venom serine proteinases.,Zhu Z, Liang Z, Zhang T, Zhu Z, Xu W, Teng M, Niu L J Biol Chem. 2005 Mar 18;280(11):10524-9. Epub 2005 Jan 4. PMID:15632114[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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