PDBsum entry 1ldp

Complex (mhc i/peptide)

PDB id: 1ldp

Contents

Protein chains

272 a.a. *

99 a.a. *

Ligands

ALA-PRO-ALA-ALA-ALA-ALA-ALA-ALA-MET

GLN-LEU-SER-PRO-PHE-PRO-PHE-ASP-LEU

NAG-NDG

NAG

* Residue conservation analysis

PDB id:

1ldp

Name:

Complex (mhc i/peptide)

Title:

Crystal structure of murine mhc class i h-2ld with a mixture of bound peptides

Structure:

Mhc class i h-2ld. Chain: h. Fragment: chain h is the heavy chain, peptide binding domain, chain l is the light chain or beta-2-microglobulin. Engineered: yes. Mutation: yes. Other_details: asparagine linked n-acetyl-glucosamine carbohydrates at chain h, n86 and n176. Mhc class i h-2ld.

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Cell: most nucleated cells. Cellular_location: cytoplasm, er, cell surface. Gene: h-2ld. Expressed in: drosophila melanogaster. Expression_system_taxid: 7227. Drosophila melanogaster.

Biol. unit:

Octamer (from PQS)

Resolution:

3.10Å R-factor: 0.221 R-free: 0.371

Authors:

J.A.Speir,I.A.Wilson

Key ref:

J.A.Speir et al. (1998). Structural basis of 2C TCR allorecognition of H-2Ld peptide complexes. Immunity, 8, 553-562. PubMed id: 9620676 DOI: 10.1016/S1074-7613(00)80560-9

Date:

15-Mar-98 Release date: 17-Jun-98

Protein chain

P01897  (HA1L_MOUSE) -  H-2 class I histocompatibility antigen, L-D alpha chain from Mus musculus

Seq: 362 a.a.

Struc: 272 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 1 residue position (black cross)

DOI no: 10.1016/S1074-7613(00)80560-9

Immunity 8:553-562 (1998)

PubMed id: 9620676

Structural basis of 2C TCR allorecognition of H-2Ld peptide complexes.

J.A.Speir, K.C.Garcia, A.Brunmark, M.Degano, P.A.Peterson, L.Teyton, I.A.Wilson.

ABSTRACT

MHC class I H-2Ld complexed with peptide QL9 (or p2Ca) is a high-affinity alloantigen for the 2C TCR. We used the crystal structure of H-2Ld with a mixture of bound peptides at 3.1 A to construct a model of the allogeneic 2C-Ld/QL9 complex for comparison with the syngeneic 2C-Kb/dEV8 structure. A prominent ridge on the floor of the Ld peptide-binding groove, not present in Kb, creates a C-terminal bulge in Ld peptides that greatly increases interactions with the 2C beta-chain. Furthermore, weak electrostatic complementarity between Asp77 on the alpha1 helix of Kb and 2C is enhanced in the allogeneic complex by closer proximity of QL9 peptide residue AspP8 to the 2C HV4 loop.

Selected figure(s)

Figure 1.
Figure 1. Ribbon Diagram of and Peptide Binding Groove Electron Density in the H-2L^d Crystal Structure(A) Ribbon diagram of the H-2L^d crystal structure viewed along the peptide-binding groove. The peptide N-terminus is shown oriented toward the viewer. (B) The peptide electron density in the H-2L^d crystal structure. The σ[A]-weighted 2F[o]-F[c] electron density is viewed with the peptide (APAAAAAAM) N-terminus on the right to show the effect of the large polymorphic residues (e.g., Trp73, Trp97, Tyr99) on the peptide conformation. Residues below the peptide from three of the α[1]α[2] domain β-strands and β[2]m (Trp60) form the bottom of the peptide-binding groove. The map is contoured at 1.5σ with a cover radius of 2.5 Å applied.

Figure 2.
Figure 2. Structure Comparison of Selected Class I MHC-Bound PeptidesThe MHC allele and peptide sequence are given above the corresponding model. The peptides were superimposed (bottom) by aligning only the α[1]α[2] C^α atoms of the MHC molecules. The L^d tube diameter is enlarged in this superimposition for clarity. The K^b peptide (dEV8) is one residue shorter (P1–P8) than the others (P1–P9).

The above figures are reprinted by permission from Cell Press: Immunity (1998, 8, 553-562) copyright 1998.

Figures were selected by an automated process.