3qr1
From Proteopedia
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- | [[ | + | ==Crystal Structure of L. pealei PLC21== |
+ | <StructureSection load='3qr1' size='340' side='right' caption='[[3qr1]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3qr1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Doryteuthis_pealeii Doryteuthis pealeii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QR1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QR1 FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br> | ||
+ | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qr0|3qr0]]</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=3qr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qr1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qr1 RCSB], [http://www.ebi.ac.uk/pdbsum/3qr1 PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The enzyme phospholipase C-beta (PLCbeta) is a crucial regulator of intracellular calcium levels whose activity is controlled by heptahelical receptors that couple to members of the G(q) family of heterotrimeric G proteins. We have determined atomic structures of two invertebrate homologs of PLCbeta (PLC21) from cephalopod retina and identified a helix from the C-terminal regulatory region that interacts with a conserved surface of the catalytic core of the enzyme. Mutations designed to disrupt the analogous interaction in human PLCbeta3 considerably increase basal activity and diminish stimulation by Galpha(q). Galpha(q) binding requires displacement of the autoinhibitory helix from the catalytic core, thus providing an allosteric mechanism for activation of PLCbeta. | ||
- | + | An autoinhibitory helix in the C-terminal region of phospholipase C-beta mediates Galpha(q) activation.,Lyon AM, Tesmer VM, Dhamsania VD, Thal DM, Gutierrez J, Chowdhury S, Suddala KC, Northup JK, Tesmer JJ Nat Struct Mol Biol. 2011 Aug 7;18(9):999-1005. doi: 10.1038/nsmb.2095. PMID:21822282<ref>PMID:21822282</ref> | |
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- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
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- | == | + | |
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[[Category: Doryteuthis pealeii]] | [[Category: Doryteuthis pealeii]] | ||
[[Category: Lyon, A M.]] | [[Category: Lyon, A M.]] |
Revision as of 05:26, 4 June 2014
Crystal Structure of L. pealei PLC21
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