1p7o

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==Crystal structure of phospholipase A2 (MIPLA4) from Micropechis ikaheka==
==Crystal structure of phospholipase A2 (MIPLA4) from Micropechis ikaheka==
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<StructureSection load='1p7o' size='340' side='right' caption='[[1p7o]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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<StructureSection load='1p7o' size='340' side='right'caption='[[1p7o]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1p7o]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Micropechis_ikaheka Micropechis ikaheka]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P7O FirstGlance]. <br>
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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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></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]] 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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p7o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p7o OCA], [http://pdbe.org/1p7o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p7o RCSB], [http://www.ebi.ac.uk/pdbsum/1p7o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1p7o ProSAT]</span></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>
</table>
</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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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].
</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].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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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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:15720395<ref>PMID:15720395</ref>
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==See Also==
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*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
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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 1p7o" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Micropechis ikaheka]]
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[[Category: Large Structures]]
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[[Category: Lok, S M]]
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[[Category: Micropechis ikaheca]]
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[[Category: Swaminathan, K]]
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[[Category: Lok SM]]
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[[Category: Hydrolase]]
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[[Category: Swaminathan K]]
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[[Category: Pancreatic loop]]
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[[Category: Phospholipase a2]]
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Current revision

Crystal structure of phospholipase A2 (MIPLA4) from Micropechis ikaheka

PDB ID 1p7o

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