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1p7o

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(New page: 200px<br /><applet load="1p7o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p7o, resolution 2.30&Aring;" /> '''Crystal structure of...)
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[[Image:1p7o.jpg|left|200px]]<br /><applet load="1p7o" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1p7o, resolution 2.30&Aring;" />
 
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'''Crystal structure of phospholipase A2 (MIPLA4) from Micropechis ikaheka'''<br />
 
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==Overview==
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==Crystal structure of phospholipase A2 (MIPLA4) from Micropechis ikaheka==
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Comparison of the crystal structures of three Micropechis ikaheka, phospholipase A2 isoenzymes (MiPLA2, MiPLA3 and MiPLA4, which exhibit, different levels of pharmacological effects) shows that their C-terminus, (residues 110-124) is the most variable. M-Type receptor binding affinity, of the isoenzymes has also been investigated and MiPLA4 binds to the, rabbit M-type receptor with high affinity. Examination of surface charges, of the isoenzymes reveals a trend of increase in positive charges with, potency. The isoenzymes are shown to oligomerize in a, concentration-dependent manner in a semi-denaturing gel. The C-termini of, the medium (MiPLA4) and highly potent (MiPLA2) isoenzyme molecules cluster, together, forming a highly exposed area. A BLAST search using the sequence, of the most potent MiPLA2 results in high similarity to Staphylococcus, aureus clotting factor A and cadherin 11. This might explain the, myotoxicity, anticoagulant and hemoglobinuria effects of MiPLA2s.
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<StructureSection load='1p7o' size='340' side='right'caption='[[1p7o]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1p7o]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Micropechis_ikaheca Micropechis ikaheca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P7O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P7O FirstGlance]. <br>
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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]] 2.3&#8491;</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=1p7o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p7o OCA], [https://pdbe.org/1p7o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p7o RCSB], [https://www.ebi.ac.uk/pdbsum/1p7o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p7o ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PA2A2_TROCA PA2A2_TROCA] PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p7/1p7o_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1p7o ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1P7O is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Micropechis_ikaheka Micropechis ikaheka]. Active as [http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1P7O OCA].
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*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structure and function comparison of Micropechis ikaheka snake venom phospholipase A2 isoenzymes., Lok SM, Gao R, Rouault M, Lambeau G, Gopalakrishnakone P, Swaminathan K, FEBS J. 2005 Mar;272(5):1211-20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15720395 15720395]
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[[Category: Large Structures]]
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[[Category: Micropechis ikaheka]]
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[[Category: Micropechis ikaheca]]
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[[Category: Phospholipase A(2)]]
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[[Category: Lok SM]]
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[[Category: Protein complex]]
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[[Category: Swaminathan K]]
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[[Category: Lok, S.M.]]
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[[Category: Swaminathan, K.]]
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[[Category: micropechis ikaheka]]
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[[Category: pancreatic loop]]
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[[Category: phospholipase a2]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:33:30 2007''
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Current revision

Crystal structure of phospholipase A2 (MIPLA4) from Micropechis ikaheka

PDB ID 1p7o

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