1NAM

MURINE ALLOREACTIVE SCFV TCR-PEPTIDE-MHC CLASS I MOLECULE COMPLEX

Summary for 1NAM

• Entry DOI: 10.2210/pdb1nam/pdb
• Related: 1FO0 1KJ3 2VAA
• Descriptor: BM3.3 T Cell Receptor alpha-Chain, BM3.3 T Cell Receptor beta-Chain, H-2 class I histocompatibility antigen, K-B alpha chain precursor, ... (7 entities in total)
• Functional Keywords: t cell receptor, class i mhc, h-2kb, tcr-pmhc complex, alloreactivity, crossreactivity, immune system
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 5
• Total formula weight: 71004.07

Authors

Reiser, J.-B.,Darnault, C.,Gregoire, C.,Mosser, T.,Mazza, G.,Kearnay, A.,van der Merwe, P.A.,Fontecilla-Camps, J.C.,Housset, D.,Malissen, B. (deposition date: 2002-11-28, release date: 2003-03-11, Last modification date: 2024-11-06)

Primary citation

Reiser, J.-B.,Darnault, C.,Gregoire, C.,Mosser, T.,Mazza, G.,Kearnay, A.,van der Merwe, P.A.,Fontecilla-Camps, J.C.,Housset, D.,Malissen, B.
CDR3 loop flexibility contributes to the degeneracy of TCR recognition
Nat.Immunol., 4:241-247, 2003

PubMed Abstract: T cell receptor (TCR) binding degeneracy lies at the heart of several physiological and pathological phenomena, yet its structural basis is poorly understood. We determined the crystal structure of a complex involving the BM3.3 TCR and an octapeptide (VSV8) bound to the H-2K(b) major histocompatibility complex molecule at a 2.7 A resolution, and compared it with the BM3.3 TCR bound to the H-2K(b) molecule loaded with a peptide that has no primary sequence identity with VSV8. Comparison of these structures showed that the BM3.3 TCR complementarity-determining region (CDR) 3alpha could undergo rearrangements to adapt to structurally different peptide residues. Therefore, CDR3 loop flexibility helps explain TCR binding cross-reactivity.

PubMed: 12563259
DOI: 10.1038/ni891

Experimental method

X-RAY DIFFRACTION (2.7 Å)