3QZW

Plasticity of human CD8 binding to peptide-HLA-A*2402

Summary for 3QZW

• Entry DOI: 10.2210/pdb3qzw/pdb
• Related: 3NFJ
• Descriptor: HLA class I histocompatibility antigen, A-24 alpha chain, Beta-2-microglobulin, 10-mer peptide from Protein Nef, ... (5 entities in total)
• Functional Keywords: immunoglobulin family, immune system, coreceptor
• Biological source: Homo sapiens (human); More
• Cellular location: Membrane; Single-pass type I membrane protein: P05534; Secreted: P61769; Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Secreted: P01732
• Total number of polymer chains: 10
• Total formula weight: 140841.72

Authors

Shi, Y.,Qi, J.,Gao, G.F. (deposition date: 2011-03-07, release date: 2011-06-29, Last modification date: 2024-10-30)

Primary citation

Shi, Y.,Qi, J.,Iwamoto, A.,Gao, G.F.
Plasticity of human CD8alpha alpha binding to peptide-HLA-A*2402
Mol.Immunol., 48:2198-2202, 2011

PubMed Abstract: The human CD8 functions as a co-receptor for specific T cell recognition, and only one complex structure of human CD8αα binding to HLA-A*0201 has been solved, revealing the molecular basis of CD8 interacting with its ligand pHLA. Here, we present the complex structures of human CD8αα bound to HLA-A*2402, which demonstrate two opposite α3 domain CD loop shifts (either pull or push) in the HLA heavy chain upon CD8 engagement. Taking the previously reported mouse CD8-pMHC complex structures into account, from the structural view, all of the data indicate the plasticity of CD8 binding to pMHC/HLA, which facilitates its co-receptor function for T cells. The plasticity of CD8 binding appears not to affect the specificity of TCR recognition, as no peptide conformation change extends to the pMHC interface for TCR contacting.

PubMed: 21645925
DOI: 10.1016/j.molimm.2011.05.009

Experimental method

X-RAY DIFFRACTION (2.798 Å)