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ModBase, a database of annotated comparative protein structure models, and associated resources.
Pieper, Ursula; Webb, Benjamin M; Barkan, David T; Schneidman-Duhovny, Dina; Schlessinger, Avner; Braberg, Hannes; Yang, Zheng; Meng, Elaine C; Pettersen, Eric F; Huang, Conrad C; Datta, Ruchira S; Sampathkumar, Parthasarathy; Madhusudhan, Mallur S; Sjölander, Kimmen; Ferrin, Thomas E; Burley, Stephen K; Sali, Andrej.
Afiliación
  • Pieper U; Department of Bioengineering and Therapeutic Sciences, Department of Pharmaceutical Chemistry, and California Institute for Quantitative Biosciences, University of California at San Francisco, CA 94158, USA.
Nucleic Acids Res ; 39(Database issue): D465-74, 2011 Jan.
Article en En | MEDLINE | ID: mdl-21097780
ModBase (http://salilab.org/modbase) is a database of annotated comparative protein structure models. The models are calculated by ModPipe, an automated modeling pipeline that relies primarily on Modeller for fold assignment, sequence-structure alignment, model building and model assessment (http://salilab.org/modeller/). ModBase currently contains 10,355,444 reliable models for domains in 2,421,920 unique protein sequences. ModBase allows users to update comparative models on demand, and request modeling of additional sequences through an interface to the ModWeb modeling server (http://salilab.org/modweb). ModBase models are available through the ModBase interface as well as the Protein Model Portal (http://www.proteinmodelportal.org/). Recently developed associated resources include the SALIGN server for multiple sequence and structure alignment (http://salilab.org/salign), the ModEval server for predicting the accuracy of protein structure models (http://salilab.org/modeval), the PCSS server for predicting which peptides bind to a given protein (http://salilab.org/pcss) and the FoXS server for calculating and fitting Small Angle X-ray Scattering profiles (http://salilab.org/foxs).
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Modelos Moleculares / Estructura Terciaria de Proteína / Bases de Datos de Proteínas Tipo de estudio: Prognostic_studies / Risk_factors_studies Idioma: En Revista: Nucleic Acids Res Año: 2011 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Modelos Moleculares / Estructura Terciaria de Proteína / Bases de Datos de Proteínas Tipo de estudio: Prognostic_studies / Risk_factors_studies Idioma: En Revista: Nucleic Acids Res Año: 2011 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido