PDBsum entry 1fzj

Immune system

PDB id: 1fzj

Contents

Protein chains

274 a.a. *

99 a.a. *

Ligands

ARG-GLY-TYR-VAL-TYR-GLN-GLY-LEU

NAG-NAG-FUL

NAG

PO4 ×2

MPD ×3

Waters ×334

* Residue conservation analysis

PDB id:

1fzj

Name:

Immune system

Title:

Mhc class i natural mutant h-2kbm1 heavy chain complexed with beta-2 microglobulin and vesicular stomatitis virus nucleoprotein

Structure:

H-2 class i histocompatibility antigen, k-b alpha chain. Chain: a. Fragment: extracellular domain. Engineered: yes. Mutation: yes. Beta-2-microglobulin. Chain: b. Engineered: yes. Nucleocapsid protein.

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: drosophila melanogaster. Expression_system_taxid: 7227. Synthetic: yes. Other_details: the peptide was chemically synthesized. The sequence of the peptide is found naturally in vesicular stomatitis virus.

Biol. unit:

Tetramer (from PQS)

Resolution:

1.90Å R-factor: 0.204 R-free: 0.222

Authors:

M.G.Rudolph,J.A.Speir,A.Brunmark,N.Mattsson,M.R.Jackson,P.A.Peterson, L.Teyton,I.A.Wilson

Key ref:

M.G.Rudolph et al. (2001). 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. PubMed id: 11290333 DOI: 10.1016/S1074-7613(01)00105-4

Date:

03-Oct-00 Release date: 28-Mar-01

Protein chain

P01901  (HA1B_MOUSE) -  H-2 class I histocompatibility antigen, K-B alpha chain from Mus musculus

Seq: 369 a.a.

Struc: 274 a.a.*

Protein chain

P01887  (B2MG_MOUSE) -  Beta-2-microglobulin from Mus musculus

Seq: 119 a.a.

Struc: 99 a.a.*

* PDB and UniProt seqs differ at 5 residue positions (black crosses)

DOI no: 10.1016/S1074-7613(01)00105-4

Immunity 14:231-242 (2001)

PubMed id: 11290333

The crystal structures of K(bm1) and K(bm8) reveal that subtle changes in the peptide environment impact thermostability and alloreactivity.

M.G.Rudolph, J.A.Speir, A.Brunmark, N.Mattsson, M.R.Jackson, P.A.Peterson, L.Teyton, I.A.Wilson.

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.

Selected figure(s)

Figure 1.
Figure 1. Molecular Structure of K^b and Location of the Mutations in K^bm1 and K^bm8(A) Ribbon diagram of wild-type K^b with peptide (magenta) bound in an extended conformation within the binding groove formed by the α helices and the β sheet floor.(B) Mutated side chains in K^bm1 and K^bm8 are shown in green and orange, respectively, while wild-type side chains are shown in (A).(C) Superimposed Cα tracings of the α[1]α[2] helices of K^b-VSV8 (yellow), K^b-SEV9 (blue), K^bm1-VSV8 (magenta), K^bm1-SEV9 (red), K^bm8-VSV8 (cyan), and K^bm8-SEV9 (green). Peptide-contacting side chains from the helices, some of which have different conformations in the six complexes, are shown

Figure 5.
Figure 5. Comparison of the Interactions at the K^bm8 Mutation Site with K^bThe coloring scheme is the same as in Figure 4 except that the MHC residues at the mutation site are colored orange. The two conformers of Ser-24 in K^bm8-VSV8 are shown in orange and blue. Note the intricate hydrogen bond networks mediated by water molecules at the K^bm8 mutation sites compared to the equivalent wild-type K^b complexes

The above figures are reprinted by permission from Cell Press: Immunity (2001, 14, 231-242) copyright 2001.

Figures were selected by an automated process.