2bye

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[[Image:2bye.png|left|200px]]
 
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{{STRUCTURE_2bye| PDB=2bye | SCENE= }}
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==NMR solution structure of phospholipase c epsilon RA 1 domain==
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<StructureSection load='2bye' size='340' side='right'caption='[[2bye]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2bye]] 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=2BYE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BYE 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">Solution NMR</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=2bye FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bye OCA], [https://pdbe.org/2bye PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bye RCSB], [https://www.ebi.ac.uk/pdbsum/2bye PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bye ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[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.
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== Function ==
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===NMR SOLUTION STRUCTURE OF PHOSPHOLIPASE C EPSILON RA 1 DOMAIN===
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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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{{ABSTRACT_PUBMED_16483931}}
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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 2bye" style="background-color:#fffaf0;"></div>
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==About this Structure==
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==See Also==
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[[2bye]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BYE OCA].
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*[[Phospholipase C|Phospholipase C]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:016483931</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Bunney, T D.]]
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[[Category: Large Structures]]
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[[Category: Driscoll, P C.]]
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[[Category: Bunney TD]]
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[[Category: Esposito, D.]]
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[[Category: Driscoll PC]]
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[[Category: Gandarillas, N L.]]
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[[Category: Esposito D]]
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[[Category: Gieschik, P.]]
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[[Category: Gandarillas NL]]
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[[Category: Harris, R.]]
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[[Category: Gieschik P]]
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[[Category: Josephs, M B.]]
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[[Category: Harris R]]
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[[Category: Katan, M.]]
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[[Category: Josephs MB]]
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[[Category: Paterson, H F.]]
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[[Category: Katan M]]
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[[Category: Pearl, L H.]]
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[[Category: Paterson HF]]
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[[Category: Rodrigues-Lima, F.]]
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[[Category: Pearl LH]]
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[[Category: Roe, S M.]]
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[[Category: Rodrigues-Lima F]]
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[[Category: Lipase]]
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[[Category: Roe SM]]
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[[Category: Phospholipase c epsilon]]
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[[Category: Ras association domain]]
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[[Category: Ubiquitin superfold]]
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Current revision

NMR solution structure of phospholipase c epsilon RA 1 domain

PDB ID 2bye

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