1fo0

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fo0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fo0 OCA], [http://www.ebi.ac.uk/pdbsum/1fo0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fo0 RCSB]</span>
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[[Category: tcr-pmhc complex]]
[[Category: tcr-pmhc complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:11:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:26:44 2008''

Revision as of 17:26, 30 March 2008


PDB ID 1fo0

Drag the structure with the mouse to rotate
, resolution 2.50Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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


Overview

Many T cell receptors (TCRs) that are selected to respond to foreign peptide antigens bound to self major histocompatibility complex (MHC) molecules are also reactive with allelic variants of self-MHC molecules. This property, termed alloreactivity, causes graft rejection and graft-versus-host disease. The structural features of alloreactivity have yet to be defined. We now present a basis for this cross-reactivity, elucidated by the crystal structure of a complex involving the BM3.3 TCR and a naturally processed octapeptide bound to the H-2Kb allogeneic MHC class I molecule. A distinguishing feature of this complex is that the eleven-residue-long complementarity-determining region 3 (CDR3) found in the BM3.3 TCR alpha chain folds away from the peptide binding groove and makes no contact with the bound peptide, the latter being exclusively contacted by the BM3.3 CDR3 beta. Our results formally establish that peptide-specific, alloreactive TCRs interact with allo-MHC in a register similar to the one they use to contact self-MHC molecules.

About this Structure

1FO0 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

Crystal structure of a T cell receptor bound to an allogeneic MHC molecule., Reiser JB, Darnault C, Guimezanes A, Gregoire C, Mosser T, Schmitt-Verhulst AM, Fontecilla-Camps JC, Malissen B, Housset D, Mazza G, Nat Immunol. 2000 Oct;1(4):291-7. PMID:11017099

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