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ATLAS: A database linking binding affinities with structures for wild‐type and mutant TCR‐pMHC complexes
Author(s) -
Borrman Tyler,
Cimons Jennifer,
Cosiano Michael,
Purcaro Michael,
Pierce Brian G.,
Baker Brian M.,
Weng Zhiping
Publication year - 2017
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.25260
Subject(s) - affinities , t cell receptor , binding affinities , major histocompatibility complex , mutant , database , computational biology , atlas (anatomy) , biology , computer science , receptor , antigen , t cell , genetics , biochemistry , paleontology , immune system , gene
The ATLAS (Altered TCR Ligand Affinities and Structures) database (https://zlab.umassmed.edu/atlas/web/) is a manually curated repository containing the binding affinities for wild-type and mutant T cell receptors (TCRs) and their antigens, peptides presented by the major histocompatibility complex (pMHC). The database links experimentally measured binding affinities with the corresponding three dimensional (3D) structures for TCR-pMHC complexes. The user can browse and search affinities, structures, and experimental details for TCRs, peptides, and MHCs of interest. We expect this database to facilitate the development of next-generation protein design algorithms targeting TCR-pMHC interactions. ATLAS can be easily parsed using modeling software that builds protein structures for training and testing. As an example, we provide structural models for all mutant TCRs in ATLAS, built using the Rosetta program. Utilizing these structures, we report a correlation of 0.63 between experimentally measured changes in binding energies and our predicted changes. Proteins 2017; 85:908-916. © 2016 Wiley Periodicals, Inc.