2VLM

The Structural Dynamics and Energetics of an Immunodominant T-cell Receptor are Programmed by its Vbeta Domain

Summary for 2VLM

• Entry DOI: 10.2210/pdb2vlm/pdb
• Related: 2VLJ 2VLK 2VLR
• Descriptor: JM22 TCR ALPHA CHAIN, JM22 TCR BETA CHAIN (3 entities in total)
• Functional Keywords: immune system, host-virus interaction, immune system-receptor-complex, immunodominance, immunoglobulin domain, tcr, mhc, flu, mhc i, t-cell, complex, membrane, receptor, immune response
• Biological source: HOMO SAPIENS (HUMAN); More
• Total number of polymer chains: 2
• Total formula weight: 49810.30

Authors

Ishizuka, J.,Stewart-Jones, G.,Van der Merwe, A.,Bell, J.,McMichael, A.,Jones, Y. (deposition date: 2008-01-15, release date: 2008-01-22, Last modification date: 2024-10-23)

Primary citation

Ishizuka, J.,Stewart-Jones, G.,Van Der Merwe, A.,Bell, J.,Mcmichael, A.,Jones, Y.
The Structural Dynamics and Energetics of an Immunodominant T-Cell Receptor are Programmed by its Vbeta Domain
Immunity, 28:171-, 2008

PubMed Abstract: Immunodominant and public T cell receptor (TCR) usage is relatively common in many viral diseases yet surprising in the context of the large naive TCR repertoire. We examined the highly conserved Vbeta17:Valpha10.2 JM22 T cell response to the influenza matrix peptide (58-66)-HLA-A*0201 (HLA-A2-flu) through extensive kinetic, thermodynamic, and structural analyses. We found several conformational adjustments that accompany JM22-HLA-A2-flu binding and identified a binding "hotspot" within the Vbeta domain of the TCR. Within this hotspot, key germline-encoded CDR1 and CDR2 loop residues and a crucial but commonly coded residue in the hypervariable region of CDR3 provide the basis for the substantial bias in the selection of the germline-encoded Vbeta17 domain. The chances of having a substantial number of T cells in the naive repertoire that have HLA-A2-flu-specific Vbeta17 receptors may consequently be relatively high, thus explaining the immunodominant usage of this clonotype.

PubMed: 18275829
DOI: 10.1016/J.IMMUNI.2007.12.018

Experimental method

X-RAY DIFFRACTION (1.98 Å)