1KJ2

Murine Alloreactive ScFv TCR-Peptide-MHC Class I Molecule Complex

Summary for 1KJ2

• Entry DOI: 10.2210/pdb1kj2/pdb
• Descriptor: Allogeneic H-2Kb MHC Class I Molecule, Naturally processed octapeptide PKB1, Beta-2 microglobulin, ... (8 entities in total)
• Functional Keywords: t cell receptor, class i mhc, h-2kb, tcr-pmhc complex, allogeneic, immune system
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 10
• Total formula weight: 142980.38

Authors

Reiser, J.-B.,Gregoire, C.,Darnault, C.,Mosser, T.,Guimezanes, A.,Schmitt-Verhulst, A.-M.,Fontecilla-Camps, J.C.,Mazza, G.,Malissen, B.,Housset, D. (deposition date: 2001-12-04, release date: 2002-03-27, Last modification date: 2023-08-16)

Primary citation

Reiser, J.B.,Gregoire, C.,Darnault, C.,Mosser, T.,Guimezanes, A.,Schmitt-Verhulst, A.M.,Fontecilla-Camps, J.C.,Mazza, G.,Malissen, B.,Housset, D.
A T cell receptor CDR3beta loop undergoes conformational changes of unprecedented magnitude upon binding to a peptide/MHC class I complex.
Immunity, 16:345-354, 2002

PubMed Abstract: The elongated complementary-determining region (CDR) 3beta found in the unliganded KB5-C20 TCR protrudes from the antigen binding site and prevents its docking onto the peptide/MHC (pMHC) surface according to a canonical diagonal orientation. We now present the crystal structure of a complex involving the KB5-C20 TCR and an octapeptide bound to the allogeneic H-2K(b) MHC class I molecule. This structure reveals how a tremendously large CDR3beta conformational change allows the KB5-C20 TCR to adapt to the rather constrained pMHC surface and achieve a diagonal docking mode. This extreme case of induced fit also shows that TCR plasticity is primarily restricted to CDR3 loops and does not propagate away from the antigen binding site.

PubMed: 11911820
DOI: 10.1016/S1074-7613(02)00288-1

Experimental method

X-RAY DIFFRACTION (2.71 Å)