CDB-a database for protein heterodimeric complexes
Abstract Crystallographic structures of protein complexes are essential to develop proteomic and structural biology methods, as prediction of protein-protein interaction (PPI) sites and protein-protein docking. Such structures can aid the development of protein complexation inhibitors. Complex DataB...
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| Veröffentlicht in: | Protein engineering, design and selection design and selection, 2018-10, Vol.31 (10), p.361-365 |
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| container_title | Protein engineering, design and selection |
| container_volume | 31 |
| creator | Aker, Malka Ohanona, Shirly Fisher, Shira Katsman, Efrat Dvorkin, Shirit Kopelowitz, Efrat Goldstein, Moshe Barnett-Itzhaki, Zohar Amitay, Moshe |
| description | Abstract
Crystallographic structures of protein complexes are essential to develop proteomic and structural biology methods, as prediction of protein-protein interaction (PPI) sites and protein-protein docking. Such structures can aid the development of protein complexation inhibitors. Complex DataBase (CDB), accessible at www.jct-bioinfo.com/cdb/search, is a database web application for heterodimeric protein crystallographic complexes along with the crystallographic structures of each individual unbound protein. Direct access to crystallographic structures of protein complexes, along with provided annotations, can serve as starting point for constructing new experimental protein complexes sets of any type, for protein binding studies, and the development and evaluation of PPIs prediction methods. |
| doi_str_mv | 10.1093/protein/gzy030 |
| format | Article |
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Crystallographic structures of protein complexes are essential to develop proteomic and structural biology methods, as prediction of protein-protein interaction (PPI) sites and protein-protein docking. Such structures can aid the development of protein complexation inhibitors. Complex DataBase (CDB), accessible at www.jct-bioinfo.com/cdb/search, is a database web application for heterodimeric protein crystallographic complexes along with the crystallographic structures of each individual unbound protein. Direct access to crystallographic structures of protein complexes, along with provided annotations, can serve as starting point for constructing new experimental protein complexes sets of any type, for protein binding studies, and the development and evaluation of PPIs prediction methods.</description><identifier>ISSN: 1741-0126</identifier><identifier>EISSN: 1741-0134</identifier><identifier>DOI: 10.1093/protein/gzy030</identifier><identifier>PMID: 30452718</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><ispartof>Protein engineering, design and selection, 2018-10, Vol.31 (10), p.361-365</ispartof><rights>The Author(s) 2018. Published by Oxford University Press. All rights reserved. For Permissions, please e-mail: journals.permissions@oup.com 2018</rights><rights>The Author(s) 2018. Published by Oxford University Press. All rights reserved. For Permissions, please e-mail: journals.permissions@oup.com.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c284t-507dc2a35870992413de342e9a87b45855813359c5a7436ef7ef2dca90826dc13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,1578,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30452718$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Aker, Malka</creatorcontrib><creatorcontrib>Ohanona, Shirly</creatorcontrib><creatorcontrib>Fisher, Shira</creatorcontrib><creatorcontrib>Katsman, Efrat</creatorcontrib><creatorcontrib>Dvorkin, Shirit</creatorcontrib><creatorcontrib>Kopelowitz, Efrat</creatorcontrib><creatorcontrib>Goldstein, Moshe</creatorcontrib><creatorcontrib>Barnett-Itzhaki, Zohar</creatorcontrib><creatorcontrib>Amitay, Moshe</creatorcontrib><title>CDB-a database for protein heterodimeric complexes</title><title>Protein engineering, design and selection</title><addtitle>Protein Eng Des Sel</addtitle><description>Abstract
Crystallographic structures of protein complexes are essential to develop proteomic and structural biology methods, as prediction of protein-protein interaction (PPI) sites and protein-protein docking. Such structures can aid the development of protein complexation inhibitors. Complex DataBase (CDB), accessible at www.jct-bioinfo.com/cdb/search, is a database web application for heterodimeric protein crystallographic complexes along with the crystallographic structures of each individual unbound protein. Direct access to crystallographic structures of protein complexes, along with provided annotations, can serve as starting point for constructing new experimental protein complexes sets of any type, for protein binding studies, and the development and evaluation of PPIs prediction methods.</description><issn>1741-0126</issn><issn>1741-0134</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><recordid>eNqFkD1PwzAQhi0EoqWwMqKMMKT1t50RwqdUiQVmy3UuEJTUwU4kyq8nKKEr093wvI_uXoTOCV4SnLFVG3wH1Xb19r3DDB-gOVGcpJgwfrjfqZyhkxg_MKZSEXKMZgxzQRXRc0Tz25vUJoXt7MZGSEofksmZvEMHwRdVA6FyifNNW8MXxFN0VNo6wtk0F-j1_u4lf0zXzw9P-fU6dVTzLhVYFY5aJrTCWUY5YQUwTiGzWm240EJowpjInLCKMwmlgpIWzmZYU1k4whbocvQO93z2EDvTVNFBXdst-D4aSpjEUlJKB3Q5oi74GAOUpg1VY8POEGx-ezLTT2bsaQhcTO5-00Cxx_-KGYCrEfB9-5_sBx5IcrY</recordid><startdate>20181001</startdate><enddate>20181001</enddate><creator>Aker, Malka</creator><creator>Ohanona, Shirly</creator><creator>Fisher, Shira</creator><creator>Katsman, Efrat</creator><creator>Dvorkin, Shirit</creator><creator>Kopelowitz, Efrat</creator><creator>Goldstein, Moshe</creator><creator>Barnett-Itzhaki, Zohar</creator><creator>Amitay, Moshe</creator><general>Oxford University Press</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20181001</creationdate><title>CDB-a database for protein heterodimeric complexes</title><author>Aker, Malka ; Ohanona, Shirly ; Fisher, Shira ; Katsman, Efrat ; Dvorkin, Shirit ; Kopelowitz, Efrat ; Goldstein, Moshe ; Barnett-Itzhaki, Zohar ; Amitay, Moshe</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c284t-507dc2a35870992413de342e9a87b45855813359c5a7436ef7ef2dca90826dc13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Aker, Malka</creatorcontrib><creatorcontrib>Ohanona, Shirly</creatorcontrib><creatorcontrib>Fisher, Shira</creatorcontrib><creatorcontrib>Katsman, Efrat</creatorcontrib><creatorcontrib>Dvorkin, Shirit</creatorcontrib><creatorcontrib>Kopelowitz, Efrat</creatorcontrib><creatorcontrib>Goldstein, Moshe</creatorcontrib><creatorcontrib>Barnett-Itzhaki, Zohar</creatorcontrib><creatorcontrib>Amitay, Moshe</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Protein engineering, design and selection</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Aker, Malka</au><au>Ohanona, Shirly</au><au>Fisher, Shira</au><au>Katsman, Efrat</au><au>Dvorkin, Shirit</au><au>Kopelowitz, Efrat</au><au>Goldstein, Moshe</au><au>Barnett-Itzhaki, Zohar</au><au>Amitay, Moshe</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>CDB-a database for protein heterodimeric complexes</atitle><jtitle>Protein engineering, design and selection</jtitle><addtitle>Protein Eng Des Sel</addtitle><date>2018-10-01</date><risdate>2018</risdate><volume>31</volume><issue>10</issue><spage>361</spage><epage>365</epage><pages>361-365</pages><issn>1741-0126</issn><eissn>1741-0134</eissn><abstract>Abstract
Crystallographic structures of protein complexes are essential to develop proteomic and structural biology methods, as prediction of protein-protein interaction (PPI) sites and protein-protein docking. Such structures can aid the development of protein complexation inhibitors. Complex DataBase (CDB), accessible at www.jct-bioinfo.com/cdb/search, is a database web application for heterodimeric protein crystallographic complexes along with the crystallographic structures of each individual unbound protein. Direct access to crystallographic structures of protein complexes, along with provided annotations, can serve as starting point for constructing new experimental protein complexes sets of any type, for protein binding studies, and the development and evaluation of PPIs prediction methods.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>30452718</pmid><doi>10.1093/protein/gzy030</doi><tpages>5</tpages></addata></record> |
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| source | Oxford University Press Journals All Titles (1996-Current); EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| title | CDB-a database for protein heterodimeric complexes |
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