PDBsum entry 1l0x

Immune system

PDB id: 1l0x

Contents

Protein chains

236 a.a. *

221 a.a. *

Ligands

GOL ×3

Waters ×181

* Residue conservation analysis

PDB id:

1l0x

Name:

Immune system

Title:

Tcr beta chain complexed with streptococcal superantigen spea

Structure:

14.3.D t cell receptor beta chain. Chain: a, c. Engineered: yes. Mutation: yes. Exotoxin type a. Chain: b, d. Synonym: scarlet fever toxin, erythrogenic toxin, spe a. Engineered: yes. Mutation: yes

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: mus musculus. Expression_system_taxid: 10090. Expression_system_cell_line: j558l. Streptococcus pyogenes. Organism_taxid: 1314. Expressed in: escherichia coli.

Resolution:

2.80Å R-factor: 0.232 R-free: 0.278

Authors:

H.Li,E.J.Sundberg,R.A.Mariuzza

Key ref:

E.J.Sundberg et al. (2002). Structures of two streptococcal superantigens bound to TCR beta chains reveal diversity in the architecture of T cell signaling complexes. Structure, 10, 687-699. PubMed id: 12015151 DOI: 10.1016/S0969-2126(02)00759-1

Date:

14-Feb-02 Release date: 03-Apr-02

Protein chains

P01851  (TCB2_MOUSE) -  T-cell receptor beta-2 chain C region from Mus musculus

Seq: 173 a.a.

Struc: 236 a.a.*

Protein chains

P0DJY7  (SPEA_STRPY) -  Exotoxin type A from Streptococcus pyogenes

Seq: 250 a.a.

Struc: 221 a.a.*

* PDB and UniProt seqs differ at 33 residue positions (black crosses)

DOI no: 10.1016/S0969-2126(02)00759-1

Structure 10:687-699 (2002)

PubMed id: 12015151

Structures of two streptococcal superantigens bound to TCR beta chains reveal diversity in the architecture of T cell signaling complexes.

E.J.Sundberg, H.Li, A.S.Llera, J.K.McCormick, J.Tormo, P.M.Schlievert, K.Karjalainen, R.A.Mariuzza.

ABSTRACT

Superantigens (SAGs) crosslink MHC class II and TCR molecules, resulting in an overstimulation of T cells associated with human disease. SAGs interact with several different surfaces on MHC molecules, necessitating the formation of multiple distinct MHC-SAG-TCR ternary signaling complexes. Variability in SAG-TCR binding modes could also contribute to the structural heterogeneity of SAG-dependent signaling complexes. We report crystal structures of the streptococcal SAGs SpeA and SpeC in complex with their corresponding TCR beta chain ligands that reveal distinct TCR binding modes. The SpeC-TCR beta chain complex structure, coupled with the recently determined SpeC-HLA-DR2a complex structure, provides a model for a novel T cell signaling complex that precludes direct TCR-MHC interactions. Thus, highly efficient T cell activation may be achieved through structurally diverse strategies of TCR ligation.

Selected figure(s)

Figure 3.
Figure 3. Diverse TCR b Chain Molecular Surface Burial by Bacterial SuperantigensMolecular surface of (A) hVb2.1 buried by SpeC, (B) mVb8.2 buried by SpeA, and (C) mVb8.2 buried by SEB. Colors are as follows: CDR1 buried molecular surface, red; CDR2 and associated FR buried molecular surface, green; HV4 and associated FR buried molecular surface, yellow; CDR3 buried molecular surface, blue.

The above figure is reprinted by permission from Cell Press: Structure (2002, 10, 687-699) copyright 2002.

Figure was selected by the author.