4l1l

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{{STRUCTURE_4l1l| PDB=4l1l | SCENE= }}
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==Rat PKC C2 domain bound to CD==
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===Rat PKC C2 domain bound to CD===
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<StructureSection load='4l1l' size='340' side='right' caption='[[4l1l]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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{{ABSTRACT_PUBMED_23937054}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4l1l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L1L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4L1L FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Pkca, Prkca ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_kinase_C Protein kinase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.13 2.7.11.13] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4l1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l1l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4l1l RCSB], [http://www.ebi.ac.uk/pdbsum/4l1l PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Due to its favorable spectroscopic properties, Cd2+ is frequently used as a probe of Ca2+ sites in proteins. We investigate the ability of Cd2+ to act as a structural and functional surrogate of Ca2+ in protein-membrane interactions. C2 domain from protein kinase Calpha (C2alpha) was chosen as a paradigm for the Ca2+-dependent phosphatidylserine-binding peripheral membrane domains. We identified the Cd2+-binding sites of C2alpha using NMR spectroscopy, determined the 1.6 A crystal structure of Cd2+-bound C2alpha, and characterized metal-ion-dependent interactions between C2alpha and phospholipid membranes using fluorescence spectroscopy and ultracentrifugation experiments. We show that Cd2+ forms a tight complex with the membrane-binding loops of C2alpha but is unable to support its membrane-binding function. This is in sharp contrast with Pb2+, which is almost as effective as Ca2+ in driving the C2alpha-membrane association process. Our results provide the first direct evidence for the specific role of divalent metal ions in mediating protein-membrane interactions, have important implications for metal substitution studies in proteins, and illustrate the potential diversity of functional responses caused by toxic metal ions.
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==Function==
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Cd as a Ca Surrogate in Protein-Membrane Interactions: Isostructural but Not Isofunctional.,Morales KA, Yang Y, Long Z, Li P, Taylor AB, Hart PJ, Igumenova TI J Am Chem Soc. 2013 Aug 21. PMID:23937054<ref>PMID:23937054</ref>
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[[http://www.uniprot.org/uniprot/KPCA_RAT KPCA_RAT]] Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in positive and negative regulation of cell proliferation, apoptosis, differentiation, migration and adhesion, cardiac hypertrophy, angiogenesis, platelet function and inflammation, by directly phosphorylating targets such as RAF1, BCL2, CSPG4, TNNT2/CTNT, or activating signaling cascade involving MAPK1/3 (ERK1/2) and RAP1GAP. Depending on the cell type, is involved in cell proliferation and cell growth arrest by positive and negative regulation of the cell cycle. Can promote cell growth by phosphorylating and activating RAF1, which mediates the activation of the MAPK/ERK signaling cascade, and/or by up-regulating CDKN1A, which facilitates active cyclin-dependent kinase (CDK) complex formation. In cells stimulated by the phorbol ester PMA, can trigger a cell cycle arrest program which is associated with the accumulation of the hyper-phosphorylated growth-suppressive form of RB1 and induction of the CDK inhibitors CDKN1A and CDKN1B. Depending on the cell type, exhibits anti-apoptotic function and protects cells from apoptosis by suppressing the p53/TP53-mediated activation of IGFBP3, or mediates anti-apoptotic action by phosphorylating BCL2. During macrophage differentiation induced by macrophage colony-stimulating factor (CSF1), is translocated to the nucleus and is associated with macrophage development. After wounding, translocates from focal contacts to lamellipodia and participates in the modulation of desmosomal adhesion. Plays a role in cell motility by phosphorylating CSPG4, which induces association of CSPG4 with extensive lamellipodia at the cell periphery and polarization of the cell accompanied by increases in cell motility. Negatively regulates myocardial contractility and positively regulates angiogenesis, platelet aggregation and thrombus formation in arteries. Mediates hypertrophic growth of neonatal cardiomyocytes, in part through a MAPK1/3 (ERK1/2)-dependent signaling pathway, and upon PMA treatment, is required to induce cardiomyocyte hypertrophy up to heart failure and death, by increasing protein synthesis, protein-DNA ratio and cell surface area. Regulates cardiomyocyte function by phosphorylating cardiac troponin T (TNNT2/CTNT), which induces significant reduction in actomyosin ATPase activity, myofilament calcium sensitivity and myocardial contractility. In angiogenesis, is required for full endothelial cell migration, adhesion to vitronectin (VTN), and vascular endothelial growth factor A (VEGFA)-dependent regulation of kinase activation and vascular tube formation. Involved in the stabilization of VEGFA mRNA at post-transcriptional level and mediates VEGFA-induced cell proliferation. In the regulation of calcium-induced platelet aggregation, mediates signals from the CD36/GP4 receptor for granule release, and activates the integrin heterodimer ITGA2B-ITGB3 through the RAP1GAP pathway for adhesion. During response to lipopolysaccharides (LPS), may regulate selective LPS-induced macrophage functions involved in host defense and inflammation. But in some inflammatory responses, may negatively regulate NF-kappa-B-induced genes, through IL1A-dependent induction of NF-kappa-B inhibitor alpha (NFKBIA/IKBA). Upon stimulation with 12-O-tetradecanoylphorbol-13-acetate (TPA), phosphorylates EIF4G1, which modulates EIF4G1 binding to MKNK1 and may be involved in the regulation of EIF4E phosphorylation. Phosphorylates KIT, leading to inhibition of KIT activity.<ref>PMID:11076962</ref> <ref>PMID:11864993</ref> <ref>PMID:15271671</ref>
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[4l1l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L1L OCA].
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</div>
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==Reference==
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==See Also==
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<ref group="xtra">PMID:023937054</ref><references group="xtra"/><references/>
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*[[Protein kinase C|Protein kinase C]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Protein kinase C]]
[[Category: Protein kinase C]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Hart, P J.]]
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[[Category: Hart, P J]]
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[[Category: Igumenova, T I.]]
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[[Category: Igumenova, T I]]
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[[Category: Li, P.]]
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[[Category: Li, P]]
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[[Category: Long, Z.]]
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[[Category: Long, Z]]
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[[Category: Morales, K M.]]
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[[Category: Morales, K M]]
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[[Category: Taylor, A B.]]
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[[Category: Taylor, A B]]
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[[Category: Yang, Y.]]
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[[Category: Yang, Y]]
[[Category: Protein kinase pkc]]
[[Category: Protein kinase pkc]]
[[Category: Transferase]]
[[Category: Transferase]]

Revision as of 15:31, 21 December 2014

Rat PKC C2 domain bound to CD

4l1l, resolution 1.60Å

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