Erratum | Published:

Crystal structure of a T cell receptor bound to an allogenic MHC molecule

Nature Immunology volume 1, page 447 (2000) | Download Citation

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Jean-Baptiste Reiser et al

Nature Immunol. 1, 291– 297 (2000).

In the October 2000 issue of Nature Immunology and were printed incorrectly, although the online version and PDF are correct. Below are the correct figures.

Figure 3. Peptide-TCR interactions occurring at the interface of four TCR-pMHC class I complexes. In this representation, the TCR-pMHC complex is viewed from the side so that the MHC α2-helix (light purple) is in the foreground and the MHC α1-helix (green) is behind the peptide (yellow). CDR2s have been removed for clarity. CDR1 and CDR3 are shown as a backbone worm diagram and color-coded as follows: CDR1α and β (green), CDR3α (dark blue), CDR3β (cyan). The peptide residues involved in contact with the TCR are shown in ball-and-stick format. The corresponding hydrogen bonds are drawn as dotted lines. This representation highlights the different bends adopted by the tip of the CDR3β loop according to the length and conformation of the MHC-bound peptide.

Figure 5. Docking of TCRs to pMHC class I ligands. All three stereoviews are looking directly onto the surface of the peptide–H-2Kbcomplex; in each, the C-terminus of the peptide is at the top. In (a) and (b), stereoviews represent the footprint of the molecular surface of the BM3.3 and 2C TCR binding sites on the peptide H-2Kbsolvent-accessible surface, respectively. The H-2Kb surface is color-coded according to the CDRs that contact it: CDR1-buried (green), CDR2-buried (red), CDR3α-buried (blue) and CDR3β-buried (cyan). The CDRs are represented as thin worms using the same color code. The peptide backbone (thick worm) and its solvent-accessible surface are depicted in yellow. The H-2Kb α-helices are visible through the semitransparent surface and colored in light emerald green (α1) or light purple (α2). In the stereoview shown in (c), the α1/α2-helices of the MHC component found in various TCR-pMHC class I complexes were superimposed to highlight the differences occurring between the respective CDR footprints on pMHC class I ligands. The MHC α-helices and the CDRs have been drawn using the same color code as in a and b. The CDRs of the different TCRs are coded as follows: BM3.3 (thicker worm and fully saturated colors), 2C (dark colors), A6 (medium intensity colors) and B7 (pale colors).

Figure 3. Peptide-TCR interactions occurring at the interface of four TCR-pMHC class I complexes. In this representation, the TCR-pMHC complex is viewed from the side so that the MHC α2-helix (light purple) is in the foreground and the MHC α1-helix (green) is behind the peptide (yellow). CDR2s have been removed for clarity. CDR1 and CDR3 are shown as a backbone worm diagram and color-coded as follows: CDR1α and β (green), CDR3α (dark blue), CDR3β (cyan). The peptide residues involved in contact with the TCR are shown in ball-and-stick format. The corresponding hydrogen bonds are drawn as dotted lines. This representation highlights the different bends adopted by the tip of the CDR3β loop according to the length and conformation of the MHC-bound peptide.

 

Figure 5. Docking of TCRs to pMHC class I ligands. All three stereoviews are looking directly onto the surface of the peptide–H-2Kbcomplex; in each, the C-terminus of the peptide is at the top. In (a) and (b), stereoviews represent the footprint of the molecular surface of the BM3.3 and 2C TCR binding sites on the peptide H-2Kbsolvent-accessible surface, respectively. The H-2Kb surface is color-coded according to the CDRs that contact it: CDR1-buried (green), CDR2-buried (red), CDR3α-buried (blue) and CDR3β-buried (cyan). The CDRs are represented as thin worms using the same color code. The peptide backbone (thick worm) and its solvent-accessible surface are depicted in yellow. The H-2Kb α-helices are visible through the semitransparent surface and colored in light emerald green (α1) or light purple (α2). In the stereoview shown in (c), the α1/α2-helices of the MHC component found in various TCR-pMHC class I complexes were superimposed to highlight the differences occurring between the respective CDR footprints on pMHC class I ligands. The MHC α-helices and the CDRs have been drawn using the same color code as in a and b. The CDRs of the different TCRs are coded as follows: BM3.3 (thicker worm and fully saturated colors), 2C (dark colors), A6 (medium intensity colors) and B7 (pale colors).

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https://doi.org/10.1038/80892

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