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The Structure of H-2K^b and K^bm8 Complexed to a Herpes Simplex Virus Determinant: Evidence for a Conformational Switch That Governs T Cell Repertoire Selection and Viral Resistance

Andrew I. Webb, Natalie A. Borg, Michelle A. Dunstone, Lars Kjer-Nielsen, Travis Beddoe, James McCluskey, Francis R. Carbone, Stephen P. Bottomley, Marie-Isabel Aguilar, Anthony W. Purcell, and Jamie Rossjohn. The Structure of H-2K^b and K^bm8 Complexed to a Herpes Simplex Virus Determinant: Evidence for a Conformational Switch That Governs T Cell Repertoire Selection and Viral Resistance. The Journal of Immunology, 2004, 173: 402–409 .

In Results, Figure 2 was incorrectly printed in grayscale. The correct color figure is shown below.

View larger version (49K): [in this window] [in a new window]   FIGURE 2. Cut-away view of the Ag-binding clefts of Kb (A) and Kbm8 (B) bound to the SSIEFARL. The 2.0- and 1.8-Å electron density omit maps of SSIEFARL complexed to the respective H-2K molecules are also indicated. Very similar conformations of the peptide were observed, highlighting the exposed Ser1, Glu4, Ala6, and Arg7 residues. Analysis of H-bond and van der Waals contacts contributed to by polymorphic amino acids in Kb (C) and Kbm8 (D) are shown in the same orientation as the views in A and B, respectively. These representations were also superimposed (E) to highlight the mobility of the Arg62 residue and the rigid-body shift in the 1 helix (residues 62–73). The Kb hc is shown in cyan, whereas Kbm8 is shown in green. The peptide ligands are shown in orange and yellow for Kb and Kbm8, respectively.

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Webb, A. I. Articles by Rossjohn, J. Search for Related Content PubMed Articles by Webb, A. I. Articles by Rossjohn, J.