The three-dimensional structure of a class I major histocompatibility complex molecule missing the alpha 3 domain of the heavy chain.

EJ Collins, DN Garboczi… - Proceedings of the …, 1995 - National Acad Sciences
Class I major histocompatibility complex (MHC) molecules are ternary complexes of the
soluble serum protein beta 2-microglobulin, MHC heavy chain, and bound peptide. The first …

Differential association of β2-microglobulin mutants with MHC class I heavy chains and structural analysis demonstrate allele-specific interactions

MJ Shields, W Hodgson, RK Ribaudo - Molecular immunology, 1999 - Elsevier
Dynamic interactions between major histocompatibility complex (MHC) class I heavy chains
and β2-microglobulin (β2m) play a critical role in their stability on the cell surface, and their …

A recombinant, soluble, single-chain class I major histocompatibility complex molecule with biological activity.

MG Mage, L Lee, RK Ribaudo, M Corr… - Proceedings of the …, 1992 - National Acad Sciences
Heterodimeric class I major histocompatibility complex molecules, which consist of a 45-kDa
heavy-chain and a 12-kDa beta 2-microglobulin (beta 2m) light chain, bind endogenously …

Characterization of an incompletely assembled major histocompatibility class I molecule (H-2Kb) associated with unusually long peptides: implications for antigen …

S Joyce, K Kuzushima, G Kepecs… - Proceedings of the …, 1994 - National Acad Sciences
We have identified two forms of a major histocompatibility complex (MHC) class I molecule,
H-2Kb, distinguishable by specific antibodies through a study of a genetically engineered …

Structural studies of class I major histocompatibility complex proteins: insights into antigen presentation

ACM Young, SG Nathenson… - The FASEB journal, 1995 - Wiley Online Library
The three‐dimensional structures of three human and two murine class I molecules, in
complex with single peptides and with mixtures of endogenous peptides, have now been …

Solution binding of an antigenic peptide to a major histocompatibility complex class I molecule and the role of beta 2-microglobulin.

LF Boyd, S Kozlowski… - Proceedings of the …, 1992 - National Acad Sciences
The major histocompatibility complex-encoded class I molecule, a noncovalent dimer of a
polymorphic 45-kDa heavy chain and a nonpolymorphic 12-kDa beta 2-microglobulin (beta …

A soluble major histocompatibility complex class I peptide-binding platform undergoes a conformational change in response to peptide epitopes

E Rigney, M Kojima, A Glithero, T Elliott - Journal of Biological Chemistry, 1998 - ASBMB
Class I major histocompatibility complexes (MHC) are heterotrimeric structures comprising
heavy chains (HC), β 2-microglobulin (β 2-m), and short antigenic peptides of 8–10 amino …

The interaction of beta 2‐microglobulin (β2m) with mouse class I major histocompatibility antigens and its ability to support peptide binding. A comparison of human …

LØ Pedersen, A Stryhn, TL Holtet… - European journal of …, 1995 - Wiley Online Library
The function of major histocompatibility complex (MHC) class I molecules is to sample
peptides derived from intracellular proteins and to present these peptides to CD8+ cytotoxic …

Peptide variants reveal how antibodies recognize major histocompatibility complex class I

KA Hogquist, AG Grandea III… - European journal of …, 1993 - Wiley Online Library
The T cell receptor (TcR) on CD8+ T lymphocytes recognizes a complex which consists of a
major histocompatibility complex (MHC) heavy chain, β2‐microglobulin (β2M), and peptide …

How do peptides associate with MHC class I molecules?

T Elliott - Immunol Today I, 1991 - cell.com
X-ray crystallographic analysis of human major histocompatibility complex (MHC) class I
glycoproteins has shown that there is extremely intimate contact between the bound peptide …