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Figure 3 | BMC Biochemistry

Figure 3

From: Side chain requirements for affinity and specificity in D5, an HIV-1 antibody derived from the VH1-69 germline segment

Figure 3

Optimized complementarity in the 25B6-5Helix interaction revealed by modeling. (a) Structural model of 25B6 complexed with 5-Helix (in cartoon) is superimposed onto the crystal structure of D5-5-Helix complex (PDB ID 2CMR). 25B6 is colored in deep olive, D5 in cyan, and 5-Helix in orange. Side chains of residues participating in the interaction are shown as stick; for 5-Helix, the side chains are colored teal in the D5-5-Helix model, and orange in the 25B6-5-Helix model. Electrostatic potential surface of 5-Helix from the 25B6 modeling is shown as well. (b) Potential of R30 in 25B6 to contact several residues on the periphery of the 5-Helix. (c) Potential interaction of E157 (5-Helix) with R50 and R53 of 25B6. (d) Potential polar interactions between 25B6 and 5-Helix mediated through D92 and D93 and a water molecule.

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