1FZM

MHC CLASS I NATURAL MUTANT H-2KBM8 HEAVY CHAIN COMPLEXED WITH BETA-2 MICROGLOBULIN AND VESICULAR STOMATITIS VIRUS NUCLEOPROTEIN

Summary for 1FZM

• Entry DOI: 10.2210/pdb1fzm/pdb
• Related: 1FZJ 1FZK 1FZO 2vaa 2vab
• Descriptor: H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN, K-B ALPHA CHAIN, PROTEIN (BETA-2-MICROGLOBULIN), PROTEIN (NUCLEOCAPSID PROTEIN), ... (9 entities in total)
• Functional Keywords: major histocompatibility complex peptide-mhc, immune system
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 3
• Total formula weight: 45583.92

Authors

Rudolph, M.G.,Speir, J.A.,Brunmark, A.,Mattsson, N.,Jackson, M.R.,Peterson, P.A.,Teyton, L.,Wilson, I.A. (deposition date: 2000-10-03, release date: 2001-03-28, Last modification date: 2024-11-20)

Primary citation

Rudolph, M.G.,Speir, J.A.,Brunmark, A.,Mattsson, N.,Jackson, M.R.,Peterson, P.A.,Teyton, L.,Wilson, I.A.
The crystal structures of K(bm1) and K(bm8) reveal that subtle changes in the peptide environment impact thermostability and alloreactivity.
Immunity, 14:231-242, 2001

PubMed Abstract: The K(bm1) and K(bm8) natural mutants of the murine MHC class I molecule H-2K(b) were originally identified by allograft rejection. They also bind viral peptides VSV8 and SEV9 with high affinity, but their peptide complexes have substantially decreased thermostability, and the K(bm1) complexes do not elicit alloreactive T cell responses. Crystal structures of the four mutant complexes at 1.7-1.9 A resolution are similar to the corresponding wild-type K(b) structures, except in the vicinity of the mutated residues, which alter the electrostatic potential, topology, hydrogen bonding, and local water structure of the peptide binding groove. Thus, these natural K(b) mutations define the minimal perturbations in the peptide environment that alter antigen presentation to T cells and abolish alloreactivity.

PubMed: 11290333
DOI: 10.1016/S1074-7613(01)00105-4

Experimental method

X-RAY DIFFRACTION (1.8 Å)