ModBase, a database of annotated comparative protein structure models and associated resources.

Abstract:

: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 almost 30 million reliable models for domains in 4.7 million unique protein sequences. ModBase allows users to compute or update comparative models on demand, through an interface to the ModWeb modeling server (http://salilab.org/modweb). ModBase models are also available through the Protein Model Portal (http://www.proteinmodelportal.org/). Recently developed associated resources include the AllosMod server for modeling ligand-induced protein dynamics (http://salilab.org/allosmod), the AllosMod-FoXS server for predicting a structural ensemble that fits an SAXS profile (http://salilab.org/allosmod-foxs), the FoXSDock server for protein-protein docking filtered by an SAXS profile (http://salilab.org/foxsdock), the SAXS Merge server for automatic merging of SAXS profiles (http://salilab.org/saxsmerge) and the Pose & Rank server for scoring protein-ligand complexes (http://salilab.org/poseandrank). In this update, we also highlight two applications of ModBase: a PSI:Biology initiative to maximize the structural coverage of the human alpha-helical transmembrane proteome and a determination of structural determinants of human immunodeficiency virus-1 protease specificity.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Pieper U,Webb BM,Dong GQ,Schneidman-Duhovny D,Fan H,Kim SJ,Khuri N,Spill YG,Weinkam P,Hammel M,Tainer JA,Nilges M,Sali A

doi

10.1093/nar/gkt1144

subject

Has Abstract

pub_date

2014-01-01 00:00:00

pages

D336-46

issue

Database issue

eissn

0305-1048

issn

1362-4962

pii

gkt1144

journal_volume

42

pub_type

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