4GKZ

HA1.7, a MHC class II restricted TCR specific for haemagglutinin

Summary for 4GKZ

• Entry DOI: 10.2210/pdb4gkz/pdb
• Descriptor: Alpha chain of Class II TCR, Beta Chain of Class II TCR, 1,2-ETHANEDIOL, ... (6 entities in total)
• Functional Keywords: major histocompatibility complex class ii (pmhc-ii), t-cell, t-cell receptor (tcr), influenza, ha1.7, immune system
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 50625.61

Authors

Holland, C.J.,Rizkallah, P.J.,Cole, D.K.,Sewell, A.K.,Godkin, A.J. (deposition date: 2012-08-13, release date: 2012-11-07, Last modification date: 2024-11-27)

Primary citation

Holland, C.J.,Rizkallah, P.J.,Vollers, S.,Calvo-Calle, J.M.,Madura, F.,Fuller, A.,Sewell, A.K.,Stern, L.J.,Godkin, A.,Cole, D.K.
Minimal conformational plasticity enables TCR cross-reactivity to different MHC class II heterodimers.
Sci Rep, 2:629-629, 2012

PubMed Abstract: Successful immunity requires that a limited pool of αβ T-cell receptors (TCRs) provide cover for a vast number of potential foreign peptide antigens presented by 'self' major histocompatibility complex (pMHC) molecules. Structures of unligated and ligated MHC class-I-restricted TCRs with different ligands, supplemented with biophysical analyses, have revealed a number of important mechanisms that govern TCR mediated antigen recognition. HA1.7 TCR binding to the influenza hemagglutinin antigen (HA(306-318)) presented by HLA-DR1 or HLA-DR4 represents an ideal system for interrogating pMHC-II antigen recognition. Accordingly, we solved the structure of the unligated HA1.7 TCR and compared it to both complex structures. Despite a relatively rigid binding mode, HA1.7 T-cells could tolerate mutations in key contact residues within the peptide epitope. Thermodynamic analysis revealed that limited plasticity and extreme favorable entropy underpinned the ability of the HA1.7 T-cell clone to cross-react with HA(306-318) presented by multiple MHC-II alleles.

PubMed: 22953050
DOI: 10.1038/srep00629

Experimental method

X-RAY DIFFRACTION (2.39 Å)