Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolution

MA Saper, PJ Bjorkman, DC Wiley - Journal of molecular biology, 1991 - Elsevier
The three-dimensional structure of the human histocompatibility antigen HLA-A2 was
determined at 3.5 Å resolution by a combination of isomorphous replacement and iterative …

Crystallization and X-ray diffraction studies on the histocompatibility antigens HLA-A2 and HLA-A28 from human cell membranes

PJ Bjorkman, JL Strominger, DC Wiley - Journal of molecular biology, 1985 - Elsevier
The human histocompatibility antigens HLA-A and HLA-B are polymorphic cell surface
glycoproteins encoded by the major histocompatibility complex. These molecules are the …

Molecular dynamics simulation of MHC-peptide complexes as a tool for predicting potential T cell epitopes

D Rognan, L Scapozza, G Folkers, A Daser - Biochemistry, 1994 - ACS Publications
Revised Manuscript Received June 13, 1994® abstract: The class I major histocompatibility
complex-encoded HLA-B* 2705 protein was simulated in complex with six different peptides …

The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHC

DR Madden, JC Gorga, JL Strominger, DC Wiley - Cell, 1992 - cell.com
Cell surface complexes of class I MHC molecules and bound peptide antigens serve as
specific recognition elements controlling the cytotoxic immune response. The 2.1 A structure …

A roadmap for hla-a, hla-b, and hla-c peptide binding specificities

G Chelvanayagam - Immunogenetics, 1996 - Springer
The high level of polymorphism in major histocompatibility complex (MHC) molecules leads
to many allele-specific peptide binding repertoires that can generally be characterized by …

[HTML][HTML] The class II MHC protein HLA-DR1 in complex with an endogenous peptide: implications for the structural basis of the specificity of peptide binding

VL Murthy, LJ Stern - Structure, 1997 - cell.com
Background: Class II major histocompatibility complex (MHC) proteins are cell surface
glycoproteins that bind peptides and present them to T cells as part of the mechanism for …

Prominent role of secondary anchor residues in peptide binding to HLA-A2. 1 molecules

J Ruppert, J Sidney, E Celis, RT Kubo, HM Grey… - Cell, 1993 - cell.com
The functional determinants of histocompatibility leukocyte antigen (HLA)-A2. 1-peptlde
interactions have been detailed by the use of quantitative molecular binding assays and a …

Comparison of the P2 specificity pocket in three human histocompatibility antigens: HLA-A* 6801, HLA-A* 0201, and HLA-B* 2705.

HC Guo, DR Madden, ML Silver… - Proceedings of the …, 1993 - National Acad Sciences
Coordinates from x-ray structures of HLA-A* 6801, HLA-A* 0201, and HLA-B* 2705 were
analyzed to examine the basis for their selectivity in peptide binding. The pocket that binds …

An altered position of the α2 helix of MHC class I is revealed by the crystal structure of HLA-B* 3501

KJ Smith, SW Reid, DI Stuart, AJ McMichael, EY Jones… - Immunity, 1996 - cell.com
The crystal structure of the human major histocompatibility complex class IB allele HLA B*
3501 complexed with the 8-mer peptide epitope HIV1 Nef 75–82 (VPLRPMTY) has been …

Structural studies on HLA-G: implications for ligand and receptor binding

CS Clements, L Kjer-Nielsen, J McCluskey… - Human immunology, 2007 - Elsevier
Human leukocyte antigen-G (HLA-G) is a class Ib major histocompatibility complex (MHC)
molecule that is specifically expressed in immune-privileged tissues. The overall structure of …