Structural highlights
Function
HA1B_MOUSE Involved in the presentation of foreign antigens to the immune system.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
CDR3 loop flexibility contributes to the degeneracy of TCR recognition.,Reiser JB, Darnault C, Gregoire C, Mosser T, Mazza G, Kearney A, van der Merwe PA, Fontecilla-Camps JC, Housset D, Malissen B Nat Immunol. 2003 Mar;4(3):241-7. Epub 2003 Feb 3. PMID:12563259[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Reiser JB, Darnault C, Gregoire C, Mosser T, Mazza G, Kearney A, van der Merwe PA, Fontecilla-Camps JC, Housset D, Malissen B. CDR3 loop flexibility contributes to the degeneracy of TCR recognition. Nat Immunol. 2003 Mar;4(3):241-7. Epub 2003 Feb 3. PMID:12563259 doi:10.1038/ni891
