Volume 91, Issue 6, Pages (December 1997)

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Volume 91, Issue 6, Pages 811-820 (December 1997) Crystallographic Analysis of Anti-p24 (HIV-1) Monoclonal Antibody Cross-Reactivity and Polyspecificity Thomas Keitel, Achim Kramer, Helga Wessner, Christa Scholz, Jens Schneider-Mergener, Wolfgang Hohne Cell Volume 91, Issue 6, Pages 811-820 (December 1997) DOI: 10.1016/S0092-8674(00)80469-9

Figure 1 Difference Electron Density Map for the h-pep/CB4-1 Complex The difference electron density was computed with the 2.60 Å resolution structure amplitudes from the CB4-1/h-pep crystal and with refined model phases from CB4-1. Density is shown for >3σ. Cell 1997 91, 811-820DOI: (10.1016/S0092-8674(00)80469-9)

Figure 2 Superposition of Variable Domains and Overlay of Complexed Peptides (A) Variable domain superposition. Residues from conserved β regions of VL (4–6, 20–25, 33–38, 45–48, 63–65, 70–74, 86–89, 102–104) were superimposed to visualize the VL/VH rearrangements. The Cα framework atoms are oriented with VL at the left. Peptides are omitted. Uncomplexed CB4-1, black; complexed with e-pep, yellow; h-pep, red; u-pep, purple; d-pep, green. (B) Peptide overlay. Superposition of VL and VH domains was performed as described in Table 2. Only the peptides are displayed: e-pep, yellow; h-pep, red; u-pep, purple; d-pep, green (N terminus: right). For a general overview of the peptides in complex with CB4-1 Fab, see Figure 4 in Kramer et al. 1997. Cell 1997 91, 811-820DOI: (10.1016/S0092-8674(00)80469-9)

Figure 3 Stereo View of the Critical Interactions of the CB4-1 Fab/Peptide Complexes The complexed peptides (green, N terminus at the right side) are orientated in the binding groove with VL at the top. (A) e-pep, GATPQDLNTnL; (B) h-pep, GATPEDLNQKLAGN; (C) u-pep, GLYEWGGARITNTD; (D) d-pep, efslkGpllqwrsG. Only those side chains of CB4-1 that are involved in binding of at least one of the peptides are given (clockwise starting from the lower right side: H:Tyr32, H:Asp31, H:Glu33, H:His52, H:His35, H:Ser54, H:Ala58, L:Phe94, L:Asp92, L:Tyr91, L:Phe32, H:Lys95, L:Arg50, L:Tyr49, L:Arg53). Yellow, hydrophobic interaction; blue, hydrophilic interaction; blue-yellow, both hydrophobic and hydrophilic interactions; white, not involved in binding of this peptide but in other cases. The Cα backbone trace is included as a white line. Cell 1997 91, 811-820DOI: (10.1016/S0092-8674(00)80469-9)