4.8 Article

MODBASE: a database of annotated comparative protein structure models and associated resources

Journal

NUCLEIC ACIDS RESEARCH
Volume 34, Issue -, Pages D291-D295

Publisher

OXFORD UNIV PRESS
DOI: 10.1093/nar/gkj059

Keywords

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Funding

  1. NCI NIH HHS [R33 CA84699] Funding Source: Medline
  2. NIGMS NIH HHS [P50 GM062529, R01 GM054762, R01 GM 54762, GM 08284, P50 GM62529, T32 GM008284, U54 GM074945] Funding Source: Medline
  3. NATIONAL CANCER INSTITUTE [R33CA084699] Funding Source: NIH RePORTER
  4. NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [U54GM074945, P50GM062529, R01GM054762] Funding Source: NIH RePORTER

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MODBASE (http://salilab.org/modbase) is a database of annotated comparative protein structure models for all available protein sequences that can be matched to at least one known protein structure. The models are calculated by MODPIPE, an automated modeling pipeline that relies on MODELLER for fold assignment, sequence-structure alignment, model building and model assessment (http:/salilab.org/modeller). MODBASE is updated regularly to reflect the growth in protein sequence and structure databases, and improvements in the software for calculating the models. MODBASE currently contains 3094524 reliable models for domains in 1094750 out of 1817889 unique protein sequences in the UniProt database (July 5, 2005); only models based on statistically significant alignments and models assessed to have the correct fold despite insignificant alignments are included. MODBASE also allows users to generate comparative models for proteins of interest with the automated modeling server MODWEB (http://salilab.org/modweb). Our other resources integrated with MODBASE include comprehensive databases of multiple protein structure alignments (DBAli, http://salilab.org/dbali), structurally defined ligand binding sites and structurally defined binary domain interfaces (PIBASE, http://salilab.org/pibase) as well as predictions of ligand binding sites, interactions between yeast proteins, and functional consequences of human nsSNPs (LS-SNP, http://salilab.org/LS-SNP).

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