2fk9
From Proteopedia
(New page: 200px<br /><applet load="2fk9" size="350" color="white" frame="true" align="right" spinBox="true" caption="2fk9, resolution 1.75Å" /> '''Human protein kinase...) |
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==Overview== | ==Overview== | ||
| - | Protein kinase C eta (PKCeta) is one of several PKC isoforms found in | + | 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Dhe-Paganon, S.]] | [[Category: Dhe-Paganon, S.]] | ||
[[Category: Edwards, A.]] | [[Category: Edwards, A.]] | ||
| - | [[Category: Jr., P | + | [[Category: Jr., P J.Finerty.]] |
| - | [[Category: Littler, D | + | [[Category: Littler, D R.]] |
[[Category: MacKenzie, F.]] | [[Category: MacKenzie, F.]] | ||
| - | [[Category: Newman, E | + | [[Category: Newman, E M.]] |
| - | [[Category: SGC, Structural | + | [[Category: SGC, Structural Genomics Consortium.]] |
[[Category: Sundstrom, M.]] | [[Category: Sundstrom, M.]] | ||
| - | [[Category: Walker, J | + | [[Category: Walker, J R.]] |
[[Category: Weigelt, J.]] | [[Category: Weigelt, J.]] | ||
[[Category: atp-binding]] | [[Category: atp-binding]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:22:14 2008'' |
Revision as of 15:22, 21 February 2008
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Human protein kinase C, eta
Overview
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.
About this Structure
2FK9 is a Single protein structure of sequence from Homo sapiens. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 17:22:14 2008
Categories: Homo sapiens | Non-specific serine/threonine protein kinase | Single protein | Arrowsmith, C. | Bochkarev, A. | Dhe-Paganon, S. | Edwards, A. | Jr., P J.Finerty. | Littler, D R. | MacKenzie, F. | Newman, E M. | SGC, Structural Genomics Consortium. | Sundstrom, M. | Walker, J R. | Weigelt, J. | Atp-binding | Diacylglycerol binding | Kinase | Metal-binding | Nucleotide-binding | Serine/threonine-protein kinase | Sgc | Structural genomics | Structural genomics consortium | Transferase
