1G6R

A FUNCTIONAL HOT SPOT FOR ANTIGEN RECOGNITION IN A SUPERAGONIST TCR/MHC COMPLEX

Summary for 1G6R

• Entry DOI: 10.2210/pdb1g6r/pdb
• Related: 2CKB
• Descriptor: ALPHA T CELL RECEPTOR, BETA T CELL RECEPTOR, MAJOR HISTOCOMPATIBILITY COMPLEX CLASS I MOLECULE, ... (5 entities in total)
• Functional Keywords: t cell antigen receptor, major histocompatibility complex, superagonist, immune system
• Biological source: Mus musculus (house mouse); More
• Cellular location: Membrane ; Single-pass membrane protein : P01852; Membrane; Single-pass type I membrane protein: P01901; Secreted: P01887
• Total number of polymer chains: 10
• Total formula weight: 185941.85

Authors

Degano, M.,Garcia, K.C.,Apostolopoulos, V.,Rudolph, M.G.,Teyton, L.,Wilson, I.A. (deposition date: 2000-11-07, release date: 2000-11-15, Last modification date: 2024-11-13)

Primary citation

Degano, M.,Garcia, K.C.,Apostolopoulos, V.,Rudolph, M.G.,Teyton, L.,Wilson, I.A.
A functional hot spot for antigen recognition in a superagonist TCR/MHC complex.
Immunity, 12:251-261, 2000

PubMed Abstract: A longstanding question in T cell receptor signaling is how structurally similar ligands, with similar affinities, can have substantially different biological activity. The crystal structure of the 2C TCR complex of H-2Kb with superagonist peptide SIYR at 2.8 A elucidates a structural basis for TCR discrimination of altered peptide ligands. The difference in antigen potency is modulated by two cavities in the TCR combining site, formed mainly by CDRs 3alpha, 3beta, and 1beta, that complement centrally located peptide residues. This "functional hot spot" allows the TCR to finely discriminate amongst energetically similar interactions within different ligands for those in which the peptide appropriately stabilizes the TCR/pMHC complex and provides a new structural perspective for understanding differential signaling resulting from T cell cross-reactivity.

PubMed: 10755612
DOI: 10.1016/S1074-7613(00)80178-8

Experimental method

X-RAY DIFFRACTION (2.8 Å)