2fjl: Difference between revisions

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==Solution Structure of the Split PH domain in Phospholipase C-gamma1==
==Solution Structure of the Split PH domain in Phospholipase C-gamma1==
<StructureSection load='2fjl' size='340' side='right'caption='[[2fjl]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''>
<StructureSection load='2fjl' size='340' side='right'caption='[[2fjl]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2fjl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FJL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FJL FirstGlance]. <br>
<table><tr><td colspan='2'>[[2fjl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FJL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FJL 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/Phosphoinositide_phospholipase_C Phosphoinositide phospholipase C], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.11 3.1.4.11] </span></td></tr>
</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=2fjl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fjl OCA], [https://pdbe.org/2fjl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fjl RCSB], [https://www.ebi.ac.uk/pdbsum/2fjl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fjl 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=2fjl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fjl OCA], [https://pdbe.org/2fjl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fjl RCSB], [https://www.ebi.ac.uk/pdbsum/2fjl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fjl ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/PLCG1_RAT PLCG1_RAT]] Mediates the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Plays an important role in the regulation of intracellular signaling cascades. Becomes activated in response to ligand-mediated activation of receptor-type tyrosine kinases, such as PDGFRA, PDGFRB, FGFR1, FGFR2, FGFR3 and FGFR4. Plays a role in actin reorganization and cell migration (By similarity).  
[https://www.uniprot.org/uniprot/PLCG1_RAT PLCG1_RAT] Mediates the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Plays an important role in the regulation of intracellular signaling cascades. Becomes activated in response to ligand-mediated activation of receptor-type tyrosine kinases, such as PDGFRA, PDGFRB, FGFR1, FGFR2, FGFR3 and FGFR4. Plays a role in actin reorganization and cell migration (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Buffalo rat]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Phosphoinositide phospholipase C]]
[[Category: Rattus norvegicus]]
[[Category: Wen, W]]
[[Category: Wen W]]
[[Category: Zhang, M]]
[[Category: Zhang M]]
[[Category: Beta-barrel]]
[[Category: Hydrolase]]

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