PDBsum entry 1nez

Immune system

PDB id: 1nez

Contents

Protein chains

274 a.a. *

99 a.a. *

122 a.a. *

Ligands

NAG ×4

Waters ×164

* Residue conservation analysis

PDB id:

1nez

Name:

Immune system

Title:

The crystal structure of a tl/cd8aa complex at 2.1a resolution:implications for memory t cell generation, co-receptor preference and affinity

Structure:

H-2 class i histocompatibility antigen, tla(c) alpha chain. Chain: a. Synonym: tl. Engineered: yes. Beta-2-microglobulin. Chain: b. Engineered: yes. T-cell surface glycoprotein cd8 alpha chain. Chain: g, h.

Source:

Synthetic: yes. Other_details: the peptide was chemically synthesized. The sequence of the peptide is naturally found in mus musculus (mouse).. Of the peptide is naturally found in mus musculus (mouse).

Resolution:

2.10Å R-factor: 0.217 R-free: 0.279

Authors:

Y.Liu,Y.Xiong,O.V.Naidenko,J.H.Liu,R.Zhang,A.Joachimiak,M.Kronenberg, H.Cheroutre,E.L.Reinherz,J.H.Wang

Key ref:

Y.Liu et al. (2003). The crystal structure of a TL/CD8alphaalpha complex at 2.1 A resolution: implications for modulation of T cell activation and memory. Immunity, 18, 205-215. PubMed id: 12594948 DOI: 10.1016/S1074-7613(03)00027-X

Date:

12-Dec-02 Release date: 08-Apr-03

Protein chain

P14432  (HA1T_MOUSE) -  H-2 class I histocompatibility antigen, TLA(B) alpha chain from Mus musculus

Seq: 384 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.*

Protein chains

P01731  (CD8A_MOUSE) -  T-cell surface glycoprotein CD8 alpha chain from Mus musculus

Seq: 247 a.a.

Struc: 122 a.a.*

* PDB and UniProt seqs differ at 15 residue positions (black crosses)

DOI no: 10.1016/S1074-7613(03)00027-X

Immunity 18:205-215 (2003)

PubMed id: 12594948

The crystal structure of a TL/CD8alphaalpha complex at 2.1 A resolution: implications for modulation of T cell activation and memory.

Y.Liu, Y.Xiong, O.V.Naidenko, J.H.Liu, R.Zhang, A.Joachimiak, M.Kronenberg, H.Cheroutre, E.L.Reinherz, J.H.Wang.

ABSTRACT

TL is a nonclassical MHC class I molecule that modulates T cell activation through relatively high-affinity interaction with CD8alphaalpha. To investigate how the TL/CD8alphaalpha interaction influences TCR signaling, we characterized the structure of the TL/CD8alphaalpha complex using X-ray crystallography. Unlike antigen-presenting molecules, the TL antigen-binding groove is occluded by specific conformational changes. This feature eliminates antigen presentation, severely hampers direct TCR recognition, and prevents TL from participating in the TCR activation complex. At the same time, the TL/CD8alphaalpha interaction is strengthened through subtle structure changes in the TL alpha3 domain. Thus, TL functions to sequester and redirect CD8alphaalpha away from the TCR, modifying lck-dependent signaling.

Selected figure(s)

Figure 1.
Figure 1. Overall View of the TL/CD8##Com- plex Structure in Ribbon Drawing Prepared with MOLSCRIPT (Krulis, 1991)

Figure 2.
Figure 2. TL-Specific Amino Acid Residues that Seal the ``Antigen Binding Groove'' in TL

The above figures are reprinted by permission from Cell Press: Immunity (2003, 18, 205-215) copyright 2003.

Figures were selected by an automated process.