1pwo

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 3: Line 3:
<StructureSection load='1pwo' size='340' side='right'caption='[[1pwo]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='1pwo' size='340' side='right'caption='[[1pwo]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[1pwo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Micropechis_ikaheka Micropechis ikaheka]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PWO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PWO FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[1pwo]] is a 4 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=1PWO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PWO FirstGlance]. <br>
-
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] </span></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</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=1pwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pwo OCA], [https://pdbe.org/1pwo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pwo RCSB], [https://www.ebi.ac.uk/pdbsum/1pwo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pwo ProSAT]</span></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=1pwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pwo OCA], [https://pdbe.org/1pwo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pwo RCSB], [https://www.ebi.ac.uk/pdbsum/1pwo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pwo ProSAT]</span></td></tr>
</table>
</table>
Line 17: Line 17:
</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=1pwo 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=1pwo ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
-
<div style="background-color:#fffaf0;">
 
-
== Publication Abstract from PubMed ==
 
-
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.
 
- 
-
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>
 
- 
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
-
</div>
 
-
<div class="pdbe-citations 1pwo" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
-
== References ==
 
-
<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Micropechis ikaheka]]
+
[[Category: Micropechis ikaheca]]
-
[[Category: Lok, S M]]
+
[[Category: Lok SM]]
-
[[Category: Swaminathan, K]]
+
[[Category: Swaminathan K]]
-
[[Category: Hydrolase]]
+
-
[[Category: Pancreatic loop]]
+
-
[[Category: Phospholipase a2]]
+

Revision as of 06:11, 3 April 2024

Crystal Structure of Phospholipase A2 (MIPLA2) from Micropechis Ikaheka

PDB ID 1pwo

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools