Crystal structures of two viral peptides in complex with murine MHC class I H-2Kb.
@article{Fremont1992CrystalSO,
title={Crystal structures of two viral peptides in complex with murine MHC class I H-2Kb.},
author={Daved H. Fremont and M. Matsumura and Enrico A. Stura and Per A. Peterson and Ian A. Wilson},
journal={Science},
year={1992},
volume={257 5072},
pages={
919-27
}
}The x-ray structures of a murine MHC class I molecule (H-2Kb) were determined in complex with two different viral peptides, derived from the vesicular stomatitis virus nucleoprotein (52-59), VSV-8, and the Sendai virus nucleoprotein (324-332), SEV-9. The H-2Kb complexes were refined at 2.3 A for VSV-8 and 2.5 A for SEV-9. The structure of H-2Kb exhibits a high degree of similarity with human HLA class I, although the individual domains can have slightly altered dispositions. Both peptides bind…
859 Citations
The H-2Kk MHC Peptide-Binding Groove Anchors the Backbone of an Octameric Antigenic Peptide in an Unprecedented Mode12
- Biology, ChemistryThe Journal of Immunology
- 2005
These two H-2Kk-peptide complexes provide insights into the mechanisms through which MHC polymorphism outside primary peptide pockets influences the conformation of the bound peptides and have implications for TCR recognition and vaccine design.
The antigenic identity of peptide-MHC complexes: A comparison of the conformations of five viral peptides presented by HLA-A2
- Biology, ChemistryCell
- 1993
Structural Definition of the H-2Kd Peptide-binding Motif*
- BiologyJournal of Biological Chemistry
- 2006
The crystal structure of the MHC class I protein H-2Kd (Kd) expressed by BALB/c mice in complex with an antigenic peptide derived from influenza A/PR/8/34 nucleoprotein (Flu, residues 147-155, TYQRTRALV) is presented.
Three-dimensional structure of H-2Dd complexed with an immunodominant peptide from human immunodeficiency virus envelope glycoprotein 120.
- Biology, ChemistryJournal of molecular biology
- 1998
A comparison of H-2Dd/P18-I10 with other MHC class I/peptide complexes of known structure provides insights into the possible basis for the specificity of the natural killer cell receptor Ly-49A for several related class I molecules.
Zooming in on the hydrophobic ridge of H-2D(b): implications for the conformational variability of bound peptides.
- Biology, ChemistryJournal of molecular biology
- 2001
Comparison with previously solved crystal structures of peptide/H-2D(b) complexes shows that the hydrophobic ridge focuses the conformational variability of the bound peptides in a "hot-spot" which could allow optimal TCR interaction and discrimination, suggesting a functional reason for the conservation of this structural element.
Endogenous peptides of a soluble major histocompatibility complex class I molecule, H-2Lds: sequence motif, quantitative binding, and molecular modeling of the complex
- BiologyThe Journal of experimental medicine
- 1992
Comparison of primary and tertiary structures of bound self and antigenic peptides revealed that residues 2 and 9 were not only restricted in sequence and tolerant of conservative substitutions, but were spatially constrained in the three-dimensional models.
The Structure and Stability of an HLA-A*0201/Octameric Tax Peptide Complex with an Empty Conserved Peptide-N-Terminal Binding Site1
- Biology, ChemistryThe Journal of Immunology
- 2000
The crystal structure of the human class I MHC molecule HLA-A2 complexed with of an octameric peptide, Tax8 (LFGYPVYV), from human T cell lymphotrophic virus-1 (HTLV-1) has been determined. This…
Modeling the interactions of a peptide-major histocompatibility class I ligand with its receptors. I. Recognition by two αβ T cell receptors
- Biology, ChemistryJ. Comput. Aided Mol. Des.
- 2000
Three-dimensional models of the complex between an Influenza Hemagglutinin peptide and its restricting element, the mouse major histocompatibility complex (MHC) class I molecule, Kk, were built by homology modeling and subsequently refined by simulated annealing and restrained molecular dynamics, suggesting a universal docking mode for αβ TCRs to MHC-peptide complexes.
The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHC
- Biology, ChemistryCell
- 1992
Crystal structure of I-Ak in complex with a dominant epitope of lysozyme.
- Chemistry, BiologyImmunity
- 1998
References
SHOWING 1-10 OF 49 REFERENCES
Molecular modeling of an antigenic complex between a viral peptide and a class I major histocompatibility glycoprotein
- Biology, ChemistryProteins
- 1992
Computer simulation was successfully employed to explain functional data and predicts α‐helical conformation for the bound peptide and a 3‐D model is proposed for the complex between a high‐affinity nonapeptide and the H‐2 Ld receptor.
Vesicular stomatitis virus antigenic octapeptide N52-59 is anchored into the groove of the H-2Kb molecule by the side chains of three amino acids and the main-chain atoms of the amino terminus.
- Biology, ChemistryProceedings of the National Academy of Sciences of the United States of America
- 1992
Data on binding of truncated peptides show that, although the Arg-1 side chain has been assigned as a TCR contact residue, the main-chain atoms of the N-terminal amino group are most likely involved in interacting with the major histocompatibility complex molecule.
Structural evidence for induced fit as a mechanism for antibody-antigen recognition.
- Biology, ChemistryScience
- 1992
The structures of the free and antigen bound antibodies demonstrate the flexibility of the antibody combining site and provide an example of induced fit as a mechanism for antibody-antigen recognition.
Emerging principles for the recognition of peptide antigens by MHC class I molecules.
- BiologyScience
- 1992
The structures of the peptide-binding specificity pockets in the groove of murine H-2Kb as well as human histocompatibility antigen class I molecules have been analyzed and usage of a limited number of both deep and shallow pockets in multiple combinations appears to allow the binding of a broad range of peptides.
Specificity pockets for the side chains of peptide antigens in HLA-Aw68
- Biology, ChemistryNature
- 1989
It is demonstrated how polymorphism creates and alters subsites (pockets) positioned to bind peptide side chains, thereby suggesting the structural basis for allelic specificity in foreign antigen binding.
Crystal structures of an antibody to a peptide and its complex with peptide antigen at 2.8 A.
- Chemistry, BiologyScience
- 1990
The three-dimensional structures of an antibody to a peptide and its complex with the peptide antigen have been determined and enable a comparison of a specific monoclonal Fab' both in its free and antigen complexed state.
A hypothetical model of the foreign antigen binding site of Class II histocompatibility molecules
- BiologyNature
- 1988
The hypothetical class II foreign-antigen binding site presented is consistent with mutation experiments1828 and provides a structural framework for proposing peptide binding models to help understand recent peptidebinding data11,2933.
Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 A resolution.
- BiologyJournal of molecular biology
- 1991
Direct binding of influenza peptides to class I HLA molecules
- BiologyNature
- 1989
A gel filtration assay is described from which direct evidence is derived for selective binding of an influenza matrix peptide to HLA-A2 and for binding of a influenza nucleoprotein peptide for restricted influenza-specific cytotoxic T lymphocytes (CTL).
Three-dimensional structure of an antigen-antibody complex at 2.8 A resolution
- Chemistry, BiologyScience
- 1986
The 2.8 A resolution three-dimensional structure of a complex between an antigen (lysozyme) and the Fab fragment from a monoclonal antibody against lysozyme has been determined and refined by x-ray…