Fig. 3: Crystal structures of QW9 and QW9_S3T complexed with B53 and B57. | Nature Communications

Fig. 3: Crystal structures of QW9 and QW9_S3T complexed with B53 and B57.

From: Molecular basis of differential HLA class I-restricted T cell recognition of a highly networked HIV peptide

Fig. 3: Crystal structures of QW9 and QW9_S3T complexed with B53 and B57.The alternative text for this image may have been generated using AI.

a Overview of the QW9-B53 structure. The green and gray ribbons represent B53 heavy and light chains, respectively, with a transparent surface as the background. The QW9 peptide is shown as a yellow stick. b The detailed interaction between B53 and QW9. For clarity, the α2 helix of B53 is removed. Water molecules: magenta spheres; hydrogen bonds: magenta broken lines. B53 is represented as a green ribbon and QW9 as a yellow stick. Specific residues from B53 are shown as green, except for residue 97 which is shown as a red stick. c Superimposition of QW9-B57 onto QW9-B53. (Silver stick: QW9B53; yellow stick: QW9B57; magenta sticks: B53 residues; cyan sticks: B57 residues; magenta broken lines: hydrogen bonds). d Top view representation of the electrostatic potential surface of QW9-B53 and QW9-B57. Significant differences between QW9-B53 and QW9-B57 are highlighted by white circles. e Overlay of QW9_S3TB53 (cyan stick) onto QW9B53 (yellow stick) in the context of the same B53 (white ribbon). Only key hydrogen bonds (magenta broken lines) and water molecules (magenta spheres) involved in the interaction between QW9_S3T and B53 are shown. f Superimposition of QW9_S3T-B57 onto QW9_S3T-B53 (silver stick: QW9_S3TB53; yellow stick: QW9_S3TB57).

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