7lcb: Difference between revisions

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 <StructureSection load='7lcb' size='340' side='right'caption='[[7lcb]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[7lcb]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LCB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LCB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[7lcb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LCB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LCB FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=XP5:(4S,7R)-7-(HEPTANOYLOXY)-4-HYDROXY-N,N,N-TRIMETHYL-10-OXO-3,5,9-TRIOXA-4-PHOSPHAHEXADECAN-1-AMINIUM+4-OXIDE'>XP5</scene>, <scene name='pdbligand=XYV:prostratin'>XYV</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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]] 1.7&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein_kinase_C Protein kinase C], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.13 2.7.11.13] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=XP5:(4S,7R)-7-(HEPTANOYLOXY)-4-HYDROXY-N,N,N-TRIMETHYL-10-OXO-3,5,9-TRIOXA-4-PHOSPHAHEXADECAN-1-AMINIUM+4-OXIDE'>XP5</scene>, <scene name='pdbligand=XYV:prostratin'>XYV</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=7lcb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lcb OCA], [https://pdbe.org/7lcb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lcb RCSB], [https://www.ebi.ac.uk/pdbsum/7lcb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lcb ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/A0A140UHX0_RAT A0A140UHX0_RAT]] Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays contrasting roles in cell death and cell survival by functioning as a pro-apoptotic protein during DNA damage-induced apoptosis, but acting as an anti-apoptotic protein during cytokine receptor-initiated cell death, is involved in tumor suppression.[PIRNR:PIRNR000551]
+[https://www.uniprot.org/uniprot/A0A140UHX0_RAT A0A140UHX0_RAT] Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays contrasting roles in cell death and cell survival by functioning as a pro-apoptotic protein during DNA damage-induced apoptosis, but acting as an anti-apoptotic protein during cytokine receptor-initiated cell death, is involved in tumor suppression.[PIRNR:PIRNR000551]
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Diacylglycerol (DAG) is a versatile lipid whose 1,2-sn-stereoisomer serves both as second messenger in signal transduction pathways that control vital cellular processes, and as metabolic precursor for downstream signaling lipids such as phosphatidic acid. Effector proteins translocate to available DAG pools in the membranes by using conserved homology 1 (C1) domains as DAG-sensing modules. Yet, how C1 domains recognize and capture DAG in the complex environment of a biological membrane has remained unresolved for the 40 years since the discovery of Protein Kinase C (PKC) as the first member of the DAG effector cohort. Herein, we report the high-resolution crystal structures of a C1 domain (C1B from PKCdelta) complexed to DAG and to each of four potent PKC agonists that produce different biological readouts and that command intense therapeutic interest. This structural information details the mechanisms of stereospecific recognition of DAG by the C1 domains, the functional properties of the lipid-binding site, and the identities of the key residues required for the recognition and capture of DAG and exogenous agonists. Moreover, the structures of the five C1 domain complexes provide the high-resolution guides for the design of agents that modulate the activities of DAG effector proteins.
-Structural anatomy of Protein Kinase C C1 domain interactions with diacylglycerol and other agonists.,Katti SS, Krieger IV, Ann J, Lee J, Sacchettini JC, Igumenova TI Nat Commun. 2022 May 16;13(1):2695. doi: 10.1038/s41467-022-30389-2. PMID:35577811<ref>PMID:35577811</ref>
+==See Also==
+*[[Protein kinase C 3D structures|Protein kinase C 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 7lcb" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Protein kinase C]]
+[[Category: Rattus norvegicus]]
-[[Category: Katti, S S]]
+[[Category: Katti SS]]
-[[Category: Krieger, I V]]
+[[Category: Krieger IV]]
-[[Category: C1]]
-[[Category: Diacylglycerol-binding]]
-[[Category: Lipid binding protein]]
-[[Category: Lipid-binding]]
-[[Category: Zn2+ finger]]