2byf
From Proteopedia
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| - | [[Image:2byf.gif|left|200px]]<br /><applet load="2byf" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2byf" /> | ||
| - | '''NMR SOLUTION STRUCTURE OF PHOSPHOLIPASE C EPSILON RA 2 DOMAIN'''<br /> | ||
| - | == | + | ==NMR solution structure of phospholipase c epsilon RA 2 domain== |
| + | <StructureSection load='2byf' size='340' side='right'caption='[[2byf]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2byf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BYF FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2byf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2byf OCA], [https://pdbe.org/2byf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2byf RCSB], [https://www.ebi.ac.uk/pdbsum/2byf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2byf ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [https://www.uniprot.org/uniprot/PLCE1_HUMAN PLCE1_HUMAN] Familial idiopathic steroid-resistant nephrotic syndrome with diffuse mesangial sclerosis;Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis. The disease is caused by mutations affecting the gene represented in this entry. | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PLCE1_HUMAN PLCE1_HUMAN] The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. PLCE1 is a bifunctional enzyme which also regulates small GTPases of the Ras superfamily through its Ras guanine-exchange factor (RasGEF) activity. As an effector of heterotrimeric and small G-protein, it may play a role in cell survival, cell growth, actin organization and T-cell activation.<ref>PMID:11022047</ref> <ref>PMID:11395506</ref> <ref>PMID:11715024</ref> <ref>PMID:11877431</ref> <ref>PMID:12721365</ref> <ref>PMID:16537651</ref> <ref>PMID:17086182</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
Ras proteins signal to a number of distinct pathways by interacting with diverse effectors. Studies of ras/effector interactions have focused on three classes, Raf kinases, ral guanylnucleotide-exchange factors, and phosphatidylinositol-3-kinases. Here we describe ras interactions with another effector, the recently identified phospholipase C epsilon (PLCepsilon). We solved structures of PLCepsilon RA domains (RA1 and RA2) by NMR and the structure of the RA2/ras complex by X-ray crystallography. Although the similarity between ubiquitin-like folds of RA1 and RA2 proves that they are homologs, only RA2 can bind ras. Some of the features of the RA2/ras interface are unique to PLCepsilon, while the ability to make contacts with both switch I and II regions of ras is shared only with phosphatidylinositol-3-kinase. Studies of PLCepsilon regulation suggest that, in a cellular context, the RA2 domain, in a mode specific to PLCepsilon, has a role in membrane targeting with further regulatory impact on PLC activity. | Ras proteins signal to a number of distinct pathways by interacting with diverse effectors. Studies of ras/effector interactions have focused on three classes, Raf kinases, ral guanylnucleotide-exchange factors, and phosphatidylinositol-3-kinases. Here we describe ras interactions with another effector, the recently identified phospholipase C epsilon (PLCepsilon). We solved structures of PLCepsilon RA domains (RA1 and RA2) by NMR and the structure of the RA2/ras complex by X-ray crystallography. Although the similarity between ubiquitin-like folds of RA1 and RA2 proves that they are homologs, only RA2 can bind ras. Some of the features of the RA2/ras interface are unique to PLCepsilon, while the ability to make contacts with both switch I and II regions of ras is shared only with phosphatidylinositol-3-kinase. Studies of PLCepsilon regulation suggest that, in a cellular context, the RA2 domain, in a mode specific to PLCepsilon, has a role in membrane targeting with further regulatory impact on PLC activity. | ||
| - | + | Structural and mechanistic insights into ras association domains of phospholipase C epsilon.,Bunney TD, Harris R, Gandarillas NL, Josephs MB, Roe SM, Sorli SC, Paterson HF, Rodrigues-Lima F, Esposito D, Ponting CP, Gierschik P, Pearl LH, Driscoll PC, Katan M Mol Cell. 2006 Feb 17;21(4):495-507. PMID:16483931<ref>PMID:16483931</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2byf" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Phospholipase C|Phospholipase C]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Bunney TD]] | ||
| + | [[Category: Driscoll PC]] | ||
| + | [[Category: Esposito D]] | ||
| + | [[Category: Gandarillas NL]] | ||
| + | [[Category: Gieschik P]] | ||
| + | [[Category: Harris R]] | ||
| + | [[Category: Josephs MB]] | ||
| + | [[Category: Katan M]] | ||
| + | [[Category: Paterson HF]] | ||
| + | [[Category: Pearl LH]] | ||
| + | [[Category: Rodrigues-Lima F]] | ||
| + | [[Category: Roe SM]] | ||
Current revision
NMR solution structure of phospholipase c epsilon RA 2 domain
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Categories: Homo sapiens | Large Structures | Bunney TD | Driscoll PC | Esposito D | Gandarillas NL | Gieschik P | Harris R | Josephs MB | Katan M | Paterson HF | Pearl LH | Rodrigues-Lima F | Roe SM
