Cell
Volume 75, Issue 4, 19 November 1993, Pages 693-708
ArticleThe antigenic identity of peptide-MHC complexes: A comparison of the conformations of five viral peptides presented by HLA-A2
References (47)
Ribbon models of macromolecules
J. Mol. Graph.
(1987)- et al.
Antigen analog-major histocompatibility complexes act as antagonists of the T cell receptor
Cell
(1992) - et al.
Structure and refinement of penicillopepsin at 1.8 Å resolution
J. Mol. Biol.
(1983) - et al.
Peptide binding to the major histocompatibility complex molecules
Curr. Opin. Struct. Biol.
(1992) - et al.
The three-dimesional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHC
Cell
(1992) - et al.
Prominent role of secondary anchor residues in peptide binding to HLA-A2.1 molecules
Cell
(1993) - et al.
Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolution
J. Mol. Biol.
(1991) - et al.
Functional consequences of engagement of the T cell receptor by low affinity ligands
J. Immunol.
(1993) - et al.
The minimum peptide epitope from the influenza virus matrix protein
J. Immunol.
(1991) - et al.
Definition of a minimal optimal cytotoxic T-cell epitope within the hepatitis B virus nucleocapsid protein
J. Virol.
(1993)
Peptide-induced conformational changes in class I heavy chains alter major histocompatibility complex recognition
J. Exp. Med.
(1992)
A system for collection and on-line integration of X-ray diffraction data from a multiwire area detector
J. Appl. Cryst.
(1987)
Methods and programs for direct-space exploitation of geometric redundancies
Acta Cryst.
(1976)
Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1
Nature
(1993)
Free R value: a novel statistical quantity for assessing the accuracy of crystal structures
Nature
(1992)
Slow-cooling protocols for crystallographic refinement by simulated annealing
Acta Cryst.
(1990)
Major histocompatibility complex conformational epitopes are peptide specific
J. Exp. Med.
(1992)
Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules
Nature
(1991)
MERLOT, an integrated package of computer programs for the determination of crystal structures by molecular replacement
J. Appl. Cryst.
(1988)
An alternative method of solving the layer scaling equations of Hamilton, Rollett and Sparks
Acta Cryst.
(1966)
Crystal structure of two viral peptides in complex with murine MHC class I H-2Kb
Science
(1992)
HLA-A2-peptide complexes: refolding and crystallization of molecules expressed in Escherichia coli and complexed with single antigenic peptides
Cited by (671)
In silico prediction of B and T cell epitopes of infectious salmon anemia virus proteins and molecular modeling of T cell epitopes to salmon major histocompatibility complex (MHC) class I
2022, Fish and Shellfish ImmunologyCitation Excerpt :This suggests that the protein regions comprised of these epitopes are promising sites for T-cell immune recognition. The structure of the TESPALTEW/UBA*0301 complex reveals that the salmon MHC-I molecule already possesses an actual Ag-binding site where epitope peptides are accommodated in the six pockets (A–F) of p/MHC-I complexes (Fig. 2 and Supplementary Fig. 3), which were initially defined in humans [43,44]. The interactions between the ISAV-F peptides are listed in Table 11, showing that the TESPALTEW-MHC UBA*0301 complex fixes the peptide via similar interactions known in chicken/mammals [45,46].
Crystallization of SLA-2*04:02:02 complexed with a CTL epitope derived from FMDV
2020, Research in Veterinary ScienceApplication of the immunoregulatory receptor LILRB1 as a crystallisation chaperone for human class I MHC complexes
2019, Journal of Immunological Methods
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Present address: Abteilung Zellphysiologie, Max-Planck-Institut für medizinische Forschung, 69120 Heidelberg, Federal Republic of Germany.
Copyright © 1993