Plate 39 Antibody cross-reaction. DB3 antibody binding site in complex with four different cross-reacting steroid haptens. The elevation plots shown here were prepared as described in the legend to Plate 6 (C). Surface color-coding is from red (most elevated) to blue (the deepest). Crystallographic coordinates by Arevalo JH et al (1994). Journal of Molecular Biology 241: 663-680. Upper left, DB3 with progesterone; upper right DB3 with 3-aetiocholanolone (5-b-androstane-3, 17-dione); lower left, DB3 with 5-a-pregnane-3-b-hemisuccinate; lower right, DB3 with 3-progesterone-11-a-olsucinate. Haptens are shown in stick representations; carbons are color-coded white, oxygens red. It can be seen that the overall shape of the binding site does not change on engaging the cross-reacting ligands; rather, the steroids orient themselves differently with respect to the binding site cavity. At the periphery of the binding site, however, changes to the shape of the surface can be seen, due to surface side-chain rearrangements. (Kindly provided by J Novotny and M Davis, Bristol-Myers Squibb Research Institute, USA with permission.)

Plate 40 Epitopes on neuraminidase. The two energetic epitopes (NC41 and NC10) on the surface of the influenza N9 neuraminidase. The calculated 'energetic' epitopes (Tulip WR et al, (1994) Biochemistry 343: 7986-7994) were color-coded, antibody-antigen from green (residues with free energy contributions stabilizing the complex), through white ('neutral' residues), to red (residues whose contributions to the free energy of binding destabilize the complex). Although the two epitopes overlap by about 80%, their binding free energy attribution is strikingly different. (Kindly provided by J Novotny and M Davis, Bristol-Myers Squibb Research Institute, USA with permission.)

Plate 41 Superantigen. Molscript model of Staphylococcus enterotoxin A (SEA) interacting with two MHC class II molecules. SEA is colored red, MHC class II and bound peptide blue and purple, respectively. On the left-hand side MHC class II b-chain contacts the SEA coordinated zinc ion (yellow) through a histidine residue on the MHC class II b chain (His81, illustrated as ball-and-chain). The right-hand side shows the interaction between MHC class II a chain and SEA. This point of interaction is centered around a phenylalanine residue in SEA (Phe47, illustrated as ball-and-chain) and a lysine residue in MHC class II a chain (Lys39, illustrated as ball-and-chain). (Kindly provided by T Kalland, M Dohlsten, P Antonsson and Morten Sogaard with permission.)

Plate 42 Systematic Lupus erythematosus. The 'butterfly rash' seen in up to 40% of SLE patients. (Kindly provided by DA Isenberg, Bloomsbury Rheumatology Unit, UK with permission.)

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  • Unincivenet
    What are your favorite flowers? In support of warning, I like very much astromerii.
    7 years ago

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