Figure 2.

Crystal Structure of the JR4 Fab-ID1 Complex

(A) The JR4 Fab-ID1 complex and its 180° view about a vertical axis are shown in a ribbon diagram with the molecular surface displayed over the residues of the Fab involved in ID1 binding (right). The structural gp120 elements engaged in JR4 Fab binding—the ${\text{β}}^{\overline{2}}$-,β4 strand and the α1 helix—are labeled.

(B) Structural comparison of JR4 Fab-ID1 and JR4 Fab-gp120_93TH057 core_e-M48 complexes. Complexes were aligned based on the ID of gp120 and are colored in darker and lighter shades for JR4 Fab-ID1 and the JR4 Fab-gp120 interface, respectively.

(C) JR4 epitope footprints on ID1 and the gp120core_e. The gp120 residues buried at the complex interface are shown as spheres and displayed over the ribbon diagram of ID1 and the gp120core_e. The gp120 residues that contribute to JR4 Fab binding in JR4 Fab-gp120_93TH057 core_e-M48 complex but are not involved in JR4 Fab binding to ID1 are shown in red.

See also Figure S2 and Table S1.