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CCProf: exploring conformational change profile of proteins.
Chang, Che-Wei; Chou, Chai-Wei; Chang, Darby Tien-Hao.
Afiliación
  • Chang CW; Department of Electrical Engineering, National Cheng Kung University, Tainan, 70101, Taiwan.
  • Chou CW; Department of Electrical Engineering, National Cheng Kung University, Tainan, 70101, Taiwan.
  • Chang DT; Department of Electrical Engineering, National Cheng Kung University, Tainan, 70101, Taiwan darby@mail.ncku.edu.tw.
Article en En | MEDLINE | ID: mdl-27016699
ABSTRACT
In many biological processes, proteins have important interactions with various molecules such as proteins, ions or ligands. Many proteins undergo conformational changes upon these interactions, where regions with large conformational changes are critical to the interactions. This work presents the CCProf platform, which provides conformational changes of entire proteins, named conformational change profile (CCP) in the context. CCProf aims to be a platform where users can study potential causes of novel conformational changes. It provides 10 biological features, including conformational change, potential binding target site, secondary structure, conservation, disorder propensity, hydropathy propensity, sequence domain, structural domain, phosphorylation site and catalytic site. All these information are integrated into a well-aligned view, so that researchers can capture important relevance between different biological features visually. The CCProf contains 986,187 protein structure pairs for 3123 proteins. In addition, CCProf provides a 3D view in which users can see the protein structures before and after conformational changes as well as binding targets that induce conformational changes. All information (e.g. CCP, binding targets and protein structures) shown in CCProf, including intermediate data are available for download to expedite further analyses. Database URLhttp//zoro.ee.ncku.edu.tw/ccprof/.
Asunto(s)

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Proteínas / Bases de Datos de Proteínas Idioma: En Revista: Database (Oxford) Año: 2016 Tipo del documento: Article País de afiliación: Taiwán

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Proteínas / Bases de Datos de Proteínas Idioma: En Revista: Database (Oxford) Año: 2016 Tipo del documento: Article País de afiliación: Taiwán