1ijl
From Proteopedia
(Difference between revisions)
| (16 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:1ijl.jpg|left|200px]]<br /><applet load="1ijl" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1ijl, resolution 2.6Å" /> | ||
| - | '''Crystal structure of acidic phospholipase A2 from deinagkistrodon acutus'''<br /> | ||
| - | == | + | ==Crystal structure of acidic phospholipase A2 from deinagkistrodon acutus== |
| + | <StructureSection load='1ijl' size='340' side='right'caption='[[1ijl]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1ijl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinagkistrodon_acutus Deinagkistrodon acutus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IJL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IJL FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1ijl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ijl OCA], [https://pdbe.org/1ijl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ijl RCSB], [https://www.ebi.ac.uk/pdbsum/1ijl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ijl ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PA2A_DEIAC PA2A_DEIAC] Snake venom phospholipase A2 (PLA2) that inhibits ADP-induced platelet aggregation. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.<ref>PMID:8931260</ref> | ||
| + | == 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/ij/1ijl_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=1ijl ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
An acidic phospholipase A(2) was purified from Deinagkistrodon acutus (Agkistrodon acutus) which displays an inhibitory effect on platelet aggregation. The three-dimensional structure of the enzyme was determined by molecular replacement at 2.6 A resolution with a crystallographic R factor of 18.40% (R(free) = 22.50%) and reasonable stereochemistry. Two molecules in the asymmetric unit form a dimer and the dimer formation accompanies a significant conformational adaptation of segment 14-23, a constituent of the 'interface recognition site' (IRS). This probably reflects the inherent structural flexibility of the IRS. The possible expansion of the site for inhibiting platelet aggregation as proposed previously [Wang et al. (1996), J. Mol. Biol. 255, 669-676] is discussed. | An acidic phospholipase A(2) was purified from Deinagkistrodon acutus (Agkistrodon acutus) which displays an inhibitory effect on platelet aggregation. The three-dimensional structure of the enzyme was determined by molecular replacement at 2.6 A resolution with a crystallographic R factor of 18.40% (R(free) = 22.50%) and reasonable stereochemistry. Two molecules in the asymmetric unit form a dimer and the dimer formation accompanies a significant conformational adaptation of segment 14-23, a constituent of the 'interface recognition site' (IRS). This probably reflects the inherent structural flexibility of the IRS. The possible expansion of the site for inhibiting platelet aggregation as proposed previously [Wang et al. (1996), J. Mol. Biol. 255, 669-676] is discussed. | ||
| - | + | Structure of an acidic phospholipase A2 from the venom of Deinagkistrodon acutus.,Gu L, Zhang H, Song S, Zhou Y, Lin Z Acta Crystallogr D Biol Crystallogr. 2002 Jan;58(Pt 1):104-10. Epub 2001, Dec 21. PMID:11752784<ref>PMID:11752784</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1ijl" style="background-color:#fffaf0;"></div> | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ==See Also== | |
| + | *[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Deinagkistrodon acutus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Gu L]] | ||
| + | [[Category: Lin Z]] | ||
| + | [[Category: Song S]] | ||
| + | [[Category: Zhang H]] | ||
| + | [[Category: Zhou Y]] | ||
Current revision
Crystal structure of acidic phospholipase A2 from deinagkistrodon acutus
| |||||||||||
Categories: Deinagkistrodon acutus | Large Structures | Gu L | Lin Z | Song S | Zhang H | Zhou Y
