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Science 3 December 1999:
Vol. 286. no. 5446, pp. 1913 - 1921
DOI: 10.1126/science.286.5446.1913
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Research Articles

The Crystal Structure of a T Cell Receptor in Complex with Peptide and MHC Class II

Ellis L. Reinherz, 12* Kemin Tan, 12dagger Lei Tang, 12dagger Petra Kern, 12ddagger Jin-huan Liu, 12 Yi Xiong, 12 Rebecca E. Hussey, 13 Alex Smolyar, 12 Brian Hare, 5 Rongguang Zhang, 6 Andrzej Joachimiak, 6 Hsiu-Ching Chang, 12 Gerhard Wagner, 5 Jia-huai Wang 14*

The crystal structure of a complex involving the D10 T cell receptor (TCR), 16-residue foreign peptide antigen, and the I-Ak self major histocompatibility complex (MHC) class II molecule is reported at 3.2 angstrom resolution. The D10 TCR is oriented in an orthogonal mode relative to its peptide-MHC (pMHC) ligand, necessitated by the amino-terminal extension of peptide residues projecting from the MHC class II antigen-binding groove as part of a mini beta  sheet. Consequently, the disposition of D10 complementarity-determining region loops is altered relative to that of most pMHCI-specific TCRs; the latter TCRs assume a diagonal orientation, although with substantial variability. Peptide recognition, which involves P-1 to P8 residues, is dominated by the Valpha domain, which also binds to the class II MHC beta 1 helix. That docking is limited to one segment of MHC-bound peptide offers an explanation for epitope recognition and altered peptide ligand effects, suggests a structural basis for alloreactivity, and illustrates how bacterial superantigens can span the TCR-pMHCII surface.

1 Laboratory of Immunobiology, Dana-Farber Cancer Institute,
2 Department of Medicine,
3 Department of Pathology,
4 Department of Pediatrics, Harvard Medical School, Boston, MA 02115, USA.
5 Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
6 Biosciences Division, Argonne National Laboratory, Argonne, IL 60439, USA.
*   To whom correspondence should be addressed. E-mail: ellis_reinherz{at}dfci.harvard.edu; jwang{at}red.dfci.harvard.edu

dagger    These authors contributed equally to this work.

ddagger    Present address: N.V. Procter Gamble Eurocor, Temselaan 100, A128, B-1853 Strombeek-Bever, Belgium.

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J.-h. Wang, R. Meijers, Y. Xiong, J.-h. Liu, T. Sakihama, R. Zhang, A. Joachimiak, and E. L. Reinherz (2001)
PNAS 98, 10799-10804
   Abstract »    Full Text »    PDF »
Hindering auxiliary anchors are potent modulators of peptide binding and selection by I-Ak class II molecules.
R. R. Latek, S. J. Petzold, and E. R. Unanue (2000)
PNAS 97, 11460-11465
   Abstract »    Full Text »    PDF »
Diversity of T cell repertoire shaped by a single peptide ligand is critically affected by its amino acid residue at a T cell receptor contact.
Y. Fukui, T. Oono, J.-P. Cabaniols, K. Nakao, K. Hirokawa, A. Inayoshi, T. Sanui, J. Kanellopoulos, E. Iwata, M. Noda, et al. (2000)
PNAS 97, 13760-13765
   Abstract »    Full Text »    PDF »
Predominant Role of T Cell Receptor (TCR)-{alpha} Chain in Forming Preimmune TCR Repertoire Revealed by Clonal TCR Reconstitution System.
T. Yokosuka, K. Takase, M. Suzuki, Y. Nakagawa, S. Taki, H. Takahashi, T. Fujisawa, H. Arase, and T. Saito (2002)
J. Exp. Med. 195, 991-1001
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Structural Comparison of Allogeneic and Syngeneic T Cell Receptor-Peptide-Major Histocompatibility Complex Complexes: A Buried Alloreactive Mutation Subtly Alters Peptide Presentation Substantially Increasing V{beta} Interactions.
J. G. Luz, M. Huang, K. C. Garcia, M. G. Rudolph, V. Apostolopoulos, L. Teyton, and I. A. Wilson (2002)
J. Exp. Med. 195, 1175-1186
   Abstract »    Full Text »    PDF »
Structural Basis of Cytochrome c Presentation by IEk.
D. H. Fremont, S. Dai, H. Chiang, F. Crawford, P. Marrack, and J. Kappler (2002)
J. Exp. Med. 195, 1043-1052
   Abstract »    Full Text »    PDF »


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