Structure of human protein kinase C eta (PKCη) C2 domain and identification of phosphorylation sites
Protein kinase C eta (PKCη) 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 PKCη-C2 domain, which is thought to mediate anionic phospholipid sensing in the prot...
Gespeichert in:
| Veröffentlicht in: | Biochemical and biophysical research communications 2006-11, Vol.349 (4), p.1182-1189 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1189 |
|---|---|
| container_issue | 4 |
| container_start_page | 1182 |
| container_title | Biochemical and biophysical research communications |
| container_volume | 349 |
| creator | Littler, Dene R. Walker, John R. She, Yi-Min Finerty, Patrick J. Newman, Elena M. Dhe-Paganon, Sirano |
| description | Protein kinase C eta (PKCη) 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 PKCη-C2 domain, which is thought to mediate anionic phospholipid sensing in the protein, was determined at 1.75
Å 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. |
| doi_str_mv | 10.1016/j.bbrc.2006.08.160 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_68899252</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0006291X06019164</els_id><sourcerecordid>68899252</sourcerecordid><originalsourceid>FETCH-LOGICAL-c354t-752633f73ee8c8d451e1a61b677cd8f8794f6a4bbeec8cf093cf742dc6a770f53</originalsourceid><addsrcrecordid>eNp9kM1q3DAUhUVpaCY_L9BF0ao0CzuSbEsydBNM80MCCSSB7IQsXRFNx_ZUkgN5srxFnikaZqC7LC4X7jn3wPkQ-k5JSQnlp8uy74MpGSG8JLKknHxBC0paUjBK6q9oQbJSsJY-7aODGJeEUFrz9hvap7wVFWVigeA-hdmkOQCeHH6eBz3idZgS-BH_9aOOgDsMSeNfd9fd-9sJ7hi206CzrEeLvYUxeeeNTn4aNxHr5ynmCa-r7Sn6BPEI7Tm9inC824fo8fzPQ3dZ3NxeXHVnN4WpmjoVomG8qpyoAKSRtm4oUM1pz4UwVjop2tpxXfc9gJHGkbYyTtTMGq6FIK6pDtHPbW6u8G-GmNTgo4HVSo8wzVFxKduWNSwb2dZowhRjAKfWwQ86vCpK1AauWqoNXLWBq4hUGW5--rFLn_sB7P-XHc1s-L01QO744iGoaDyMBqwPYJKyk_8s_wOjnoxe</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>68899252</pqid></control><display><type>article</type><title>Structure of human protein kinase C eta (PKCη) C2 domain and identification of phosphorylation sites</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><creator>Littler, Dene R. ; Walker, John R. ; She, Yi-Min ; Finerty, Patrick J. ; Newman, Elena M. ; Dhe-Paganon, Sirano</creator><creatorcontrib>Littler, Dene R. ; Walker, John R. ; She, Yi-Min ; Finerty, Patrick J. ; Newman, Elena M. ; Dhe-Paganon, Sirano</creatorcontrib><description>Protein kinase C eta (PKCη) 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 PKCη-C2 domain, which is thought to mediate anionic phospholipid sensing in the protein, was determined at 1.75
Å 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.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2006.08.160</identifier><identifier>PMID: 16973127</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Binding Sites ; C2 domain ; Computer Simulation ; Eta ; Models, Chemical ; Models, Molecular ; Molecular Sequence Data ; Novel isoform ; Phosphorylation ; PKC ; Protein Binding ; Protein Conformation ; Protein kinase C ; Protein Kinase C - chemistry ; Protein Kinase C - ultrastructure ; Protein Structure, Tertiary ; Structure ; X-ray</subject><ispartof>Biochemical and biophysical research communications, 2006-11, Vol.349 (4), p.1182-1189</ispartof><rights>2006</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c354t-752633f73ee8c8d451e1a61b677cd8f8794f6a4bbeec8cf093cf742dc6a770f53</citedby><cites>FETCH-LOGICAL-c354t-752633f73ee8c8d451e1a61b677cd8f8794f6a4bbeec8cf093cf742dc6a770f53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006291X06019164$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16973127$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Littler, Dene R.</creatorcontrib><creatorcontrib>Walker, John R.</creatorcontrib><creatorcontrib>She, Yi-Min</creatorcontrib><creatorcontrib>Finerty, Patrick J.</creatorcontrib><creatorcontrib>Newman, Elena M.</creatorcontrib><creatorcontrib>Dhe-Paganon, Sirano</creatorcontrib><title>Structure of human protein kinase C eta (PKCη) C2 domain and identification of phosphorylation sites</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Protein kinase C eta (PKCη) 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 PKCη-C2 domain, which is thought to mediate anionic phospholipid sensing in the protein, was determined at 1.75
Å 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.</description><subject>Amino Acid Sequence</subject><subject>Binding Sites</subject><subject>C2 domain</subject><subject>Computer Simulation</subject><subject>Eta</subject><subject>Models, Chemical</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Novel isoform</subject><subject>Phosphorylation</subject><subject>PKC</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Protein kinase C</subject><subject>Protein Kinase C - chemistry</subject><subject>Protein Kinase C - ultrastructure</subject><subject>Protein Structure, Tertiary</subject><subject>Structure</subject><subject>X-ray</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kM1q3DAUhUVpaCY_L9BF0ao0CzuSbEsydBNM80MCCSSB7IQsXRFNx_ZUkgN5srxFnikaZqC7LC4X7jn3wPkQ-k5JSQnlp8uy74MpGSG8JLKknHxBC0paUjBK6q9oQbJSsJY-7aODGJeEUFrz9hvap7wVFWVigeA-hdmkOQCeHH6eBz3idZgS-BH_9aOOgDsMSeNfd9fd-9sJ7hi206CzrEeLvYUxeeeNTn4aNxHr5ynmCa-r7Sn6BPEI7Tm9inC824fo8fzPQ3dZ3NxeXHVnN4WpmjoVomG8qpyoAKSRtm4oUM1pz4UwVjop2tpxXfc9gJHGkbYyTtTMGq6FIK6pDtHPbW6u8G-GmNTgo4HVSo8wzVFxKduWNSwb2dZowhRjAKfWwQ86vCpK1AauWqoNXLWBq4hUGW5--rFLn_sB7P-XHc1s-L01QO744iGoaDyMBqwPYJKyk_8s_wOjnoxe</recordid><startdate>20061103</startdate><enddate>20061103</enddate><creator>Littler, Dene R.</creator><creator>Walker, John R.</creator><creator>She, Yi-Min</creator><creator>Finerty, Patrick J.</creator><creator>Newman, Elena M.</creator><creator>Dhe-Paganon, Sirano</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20061103</creationdate><title>Structure of human protein kinase C eta (PKCη) C2 domain and identification of phosphorylation sites</title><author>Littler, Dene R. ; Walker, John R. ; She, Yi-Min ; Finerty, Patrick J. ; Newman, Elena M. ; Dhe-Paganon, Sirano</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c354t-752633f73ee8c8d451e1a61b677cd8f8794f6a4bbeec8cf093cf742dc6a770f53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Amino Acid Sequence</topic><topic>Binding Sites</topic><topic>C2 domain</topic><topic>Computer Simulation</topic><topic>Eta</topic><topic>Models, Chemical</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Novel isoform</topic><topic>Phosphorylation</topic><topic>PKC</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Protein kinase C</topic><topic>Protein Kinase C - chemistry</topic><topic>Protein Kinase C - ultrastructure</topic><topic>Protein Structure, Tertiary</topic><topic>Structure</topic><topic>X-ray</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Littler, Dene R.</creatorcontrib><creatorcontrib>Walker, John R.</creatorcontrib><creatorcontrib>She, Yi-Min</creatorcontrib><creatorcontrib>Finerty, Patrick J.</creatorcontrib><creatorcontrib>Newman, Elena M.</creatorcontrib><creatorcontrib>Dhe-Paganon, Sirano</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Littler, Dene R.</au><au>Walker, John R.</au><au>She, Yi-Min</au><au>Finerty, Patrick J.</au><au>Newman, Elena M.</au><au>Dhe-Paganon, Sirano</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure of human protein kinase C eta (PKCη) C2 domain and identification of phosphorylation sites</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2006-11-03</date><risdate>2006</risdate><volume>349</volume><issue>4</issue><spage>1182</spage><epage>1189</epage><pages>1182-1189</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Protein kinase C eta (PKCη) 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 PKCη-C2 domain, which is thought to mediate anionic phospholipid sensing in the protein, was determined at 1.75
Å 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.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>16973127</pmid><doi>10.1016/j.bbrc.2006.08.160</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-291X |
| ispartof | Biochemical and biophysical research communications, 2006-11, Vol.349 (4), p.1182-1189 |
| issn | 0006-291X 1090-2104 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_68899252 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Amino Acid Sequence Binding Sites C2 domain Computer Simulation Eta Models, Chemical Models, Molecular Molecular Sequence Data Novel isoform Phosphorylation PKC Protein Binding Protein Conformation Protein kinase C Protein Kinase C - chemistry Protein Kinase C - ultrastructure Protein Structure, Tertiary Structure X-ray |
| title | Structure of human protein kinase C eta (PKCη) C2 domain and identification of phosphorylation sites |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-13T05%3A15%3A24IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Structure%20of%20human%20protein%20kinase%20C%20eta%20(PKC%CE%B7)%20C2%20domain%20and%20identification%20of%20phosphorylation%20sites&rft.jtitle=Biochemical%20and%20biophysical%20research%20communications&rft.au=Littler,%20Dene%20R.&rft.date=2006-11-03&rft.volume=349&rft.issue=4&rft.spage=1182&rft.epage=1189&rft.pages=1182-1189&rft.issn=0006-291X&rft.eissn=1090-2104&rft_id=info:doi/10.1016/j.bbrc.2006.08.160&rft_dat=%3Cproquest_cross%3E68899252%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=68899252&rft_id=info:pmid/16973127&rft_els_id=S0006291X06019164&rfr_iscdi=true |