2fk9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:28, 30 August 2023) (edit) (undo)
 
(12 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2fk9.gif|left|200px]]
 
-
{{Structure
+
==Human protein kinase C, eta==
-
|PDB= 2fk9 |SIZE=350|CAPTION= <scene name='initialview01'>2fk9</scene>, resolution 1.75&Aring;
+
<StructureSection load='2fk9' size='340' side='right'caption='[[2fk9]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND=
+
<table><tr><td colspan='2'>[[2fk9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FK9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FK9 FirstGlance]. <br>
-
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
-
|GENE= PRKCH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fk9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fk9 OCA], [https://pdbe.org/2fk9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fk9 RCSB], [https://www.ebi.ac.uk/pdbsum/2fk9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fk9 ProSAT]</span></td></tr>
-
|DOMAIN=
+
</table>
-
|RELATEDENTRY=
+
== Disease ==
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fk9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fk9 OCA], [http://www.ebi.ac.uk/pdbsum/2fk9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fk9 RCSB]</span>
+
[https://www.uniprot.org/uniprot/KPCL_HUMAN KPCL_HUMAN] Disease susceptibility is associated with variations affecting the gene represented in this entry.
-
}}
+
== Function ==
-
 
+
[https://www.uniprot.org/uniprot/KPCL_HUMAN KPCL_HUMAN] Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in the regulation of cell differentiation in keratinocytes and pre-B cell receptor, mediates regulation of epithelial tight junction integrity and foam cell formation, and is required for glioblastoma proliferation and apoptosis prevention in MCF-7 cells. In keratinocytes, binds and activates the tyrosine kinase FYN, which in turn blocks epidermal growth factor receptor (EGFR) signaling and leads to keratinocyte growth arrest and differentiation. Associates with the cyclin CCNE1-CDK2-CDKN1B complex and inhibits CDK2 kinase activity, leading to RB1 dephosphorylation and thereby G1 arrest in keratinocytes. In association with RALA activates actin depolymerization, which is necessary for keratinocyte differentiation. In the pre-B cell receptor signaling, functions downstream of BLNK by up-regulating IRF4, which in turn activates L chain gene rearrangement. Regulates epithelial tight junctions (TJs) by phosphorylating occludin (OCLN) on threonine residues, which is necessary for the assembly and maintenance of TJs. In association with PLD2 and via TLR4 signaling, is involved in lipopolysaccharide (LPS)-induced RGS2 down-regulation and foam cell formation. Upon PMA stimulation, mediates glioblastoma cell proliferation by activating the mTOR pathway, the PI3K/AKT pathway and the ERK1-dependent phosphorylation of ELK1. Involved in the protection of glioblastoma cells from irradiation-induced apoptosis by preventing caspase-9 activation. In camptothecin-treated MCF-7 cells, regulates NF-kappa-B upstream signaling by activating IKBKB, and confers protection against DNA damage-induced apoptosis. Promotes oncogenic functions of ATF2 in the nucleus while blocking its apoptotic function at mitochondria. Phosphorylates ATF2 which promotes its nuclear retention and transcriptional activity and negatively regulates its mitochondrial localization.<ref>PMID:11112424</ref> <ref>PMID:10806212</ref> <ref>PMID:11772428</ref> <ref>PMID:15489897</ref> <ref>PMID:17146445</ref> <ref>PMID:18780722</ref> <ref>PMID:19114660</ref> <ref>PMID:20558593</ref> <ref>PMID:21820409</ref> <ref>PMID:22304920</ref>
-
'''Human protein kinase C, eta'''
+
== Evolutionary Conservation ==
-
 
+
[[Image:Consurf_key_small.gif|200px|right]]
-
 
+
Check<jmol>
-
==Overview==
+
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fk/2fk9_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2fk9 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
Protein kinase C eta (PKCeta) is one of several PKC isoforms found in humans. It is a novel PKC isoform in that it is activated by diacylglycerol and anionic phospholipids but not calcium. The crystal structure of the PKCeta-C2 domain, which is thought to mediate anionic phospholipid sensing in the protein, was determined at 1.75 A resolution. The structure is similar to that of the PKC epsilon C2 domain but with significant variations at the putative lipid-binding site. Two serine residues within PKC eta were identified in vitro as potential autophosphorylation sites. In the unphosphorylated structure both serines line the putative lipid-binding site and may therefore play a role in the lipid-regulation of the kinase.
Protein kinase C eta (PKCeta) is one of several PKC isoforms found in humans. It is a novel PKC isoform in that it is activated by diacylglycerol and anionic phospholipids but not calcium. The crystal structure of the PKCeta-C2 domain, which is thought to mediate anionic phospholipid sensing in the protein, was determined at 1.75 A resolution. The structure is similar to that of the PKC epsilon C2 domain but with significant variations at the putative lipid-binding site. Two serine residues within PKC eta were identified in vitro as potential autophosphorylation sites. In the unphosphorylated structure both serines line the putative lipid-binding site and may therefore play a role in the lipid-regulation of the kinase.
-
==Disease==
+
Structure of human protein kinase C eta (PKCeta) C2 domain and identification of phosphorylation sites.,Littler DR, Walker JR, She YM, Finerty PJ Jr, Newman EM, Dhe-Paganon S Biochem Biophys Res Commun. 2006 Nov 3;349(4):1182-9. Epub 2006 Sep 5. PMID:16973127<ref>PMID:16973127</ref>
-
Known disease associated with this structure: Cerebral infarction, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=605437 605437]]
+
-
==About this Structure==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
2FK9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FK9 OCA].
+
</div>
 +
<div class="pdbe-citations 2fk9" style="background-color:#fffaf0;"></div>
-
==Reference==
+
==See Also==
-
Structure of human protein kinase C eta (PKCeta) C2 domain and identification of phosphorylation sites., Littler DR, Walker JR, She YM, Finerty PJ Jr, Newman EM, Dhe-Paganon S, Biochem Biophys Res Commun. 2006 Nov 3;349(4):1182-9. Epub 2006 Sep 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16973127 16973127]
+
*[[Protein kinase C 3D structures|Protein kinase C 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Non-specific serine/threonine protein kinase]]
+
[[Category: Large Structures]]
-
[[Category: Single protein]]
+
[[Category: Arrowsmith C]]
-
[[Category: Arrowsmith, C.]]
+
[[Category: Bochkarev A]]
-
[[Category: Bochkarev, A.]]
+
[[Category: Dhe-Paganon S]]
-
[[Category: Dhe-Paganon, S.]]
+
[[Category: Edwards A]]
-
[[Category: Edwards, A.]]
+
[[Category: Finerty Jr PJ]]
-
[[Category: Jr., P J.Finerty.]]
+
[[Category: Littler DR]]
-
[[Category: Littler, D R.]]
+
[[Category: MacKenzie F]]
-
[[Category: MacKenzie, F.]]
+
[[Category: Newman EM]]
-
[[Category: Newman, E M.]]
+
[[Category: Sundstrom M]]
-
[[Category: SGC, Structural Genomics Consortium.]]
+
[[Category: Walker JR]]
-
[[Category: Sundstrom, M.]]
+
[[Category: Weigelt J]]
-
[[Category: Walker, J R.]]
+
-
[[Category: Weigelt, J.]]
+
-
[[Category: atp-binding]]
+
-
[[Category: diacylglycerol binding]]
+
-
[[Category: kinase]]
+
-
[[Category: metal-binding]]
+
-
[[Category: nucleotide-binding]]
+
-
[[Category: serine/threonine-protein kinase]]
+
-
[[Category: sgc]]
+
-
[[Category: structural genomic]]
+
-
[[Category: structural genomics consortium]]
+
-
[[Category: transferase]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:04:00 2008''
+

Current revision

Human protein kinase C, eta

PDB ID 2fk9

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2fk9"
Personal tools