ISB Home



- Article -





Volume 5


Full article

In Silico Biology 5, 0046 (2005); ©2005, Bioinformation Systems e.V.  



T cell receptor/peptide/MHC molecular characterization and standardized pMHC contact sites in IMGT/3Dstructure-DB

Quentin Kaas and Marie-Paule Lefranc*

IMGT, the international ImMunoGeneTics information system®
Université Montpellier II, Laboratoire d'ImmunoGénétique Moléculaire LIGM, UPR CNRS 1142, Institut de Génétique Humaine IGH, 141 rue de la Cardonille, 34396 Montpellier Cedex 5, France


* Corresponding author
   Email: lefranc@ligm.igh.cnrs.fr    Institut Universitaire de France


Edited by E. Wingender; received September 02, 2005; revised and accepted September 18, 2005; published October 20, 2005


Abstract

One of the key elements in the adaptive immune response is the presentation of peptides by the major histocompatibility complex (MHC) to the T cell receptors (TR) at the surface of T cells. The characterization of the TR/peptide/MHC trimolecular complexes (TR/pMHC) is crucial to the fields of immunology, vaccination and immunotherapy. In order to facilitate data comparison and cross-referencing between experiments from different laboratories whatever the receptor, the chain type, the domain, or the species, IMGT, the international ImMunoGeneTics information system® (http://imgt.cines.fr), has developed IMGT-ONTOLOGY, the first ontology in immunogenetics and immunoinformatics. In IMGT/3Dstructure-DB, the IMGT three-dimensional structure database, TR/pMHC molecular characterization and pMHC contact analysis are made according to the IMGT Scientific chart rules, based on the IMGT-ONTOLOGY concepts. IMGT/3Dstructure-DB provides the standardized IMGT gene and allele names (CLASSIFICATION), the standardized IMGT labels (DESCRIPTION) and the IMGT unique numbering (NUMEROTATION). As the IMGT structural unit is the domain, amino acids at conserved positions always have the same number in the IMGT databases, tools and Web resources. For the TR alpha and beta chains, the amino acids in contact with the peptide/MHC (pMHC) are defined according to the IMGT unique numbering for V-DOMAIN. The MHC cleft that binds the peptide is formed by two groove domains (G-DOMAIN), each one comprising four antiparallel beta strands and one alpha helix. The IMGT unique numbering for G-DOMAIN applies both to the first two domains (G-ALPHA1 and G-ALPHA2) of the MHC class I alpha chain, and to the first domain (G-ALPHA and G-BETA) of the two MHC class II chains, alpha and beta. Based on the IMGT unique numbering, we defined eleven contact sites for the analysis of the pMHC contacts. The TR/pMHC contact description, based on the IMGT numbering, can be queried in the IMGT/StucturalQuery tool, at http://imgt.cines.fr.

Availability: IMGT/3Dstructure-DB is freely available at http://imgt.cines.fr.


Keywords: IMGT, T cell receptor, TR, major histocompatibility complex, MHC, pMHC, TR/peptide/MHC complex, TR/pMHC, three-dimensional structure, 3D structure, contact analysis, IMGT/3Dstructure-DB, IMGT/StructuralQuery, immunoinformatics, immunogenetics, immune system