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![[Figure 1]](ag5055fig1mag.jpg)
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Figure 1
(a) A surface representation of two Fabs related by a crystallographic twofold axis shows that their L1 loops extend into pockets normally expected to bind antigen on the other Fab. Light chain, cyan; heavy chain, slate. (b) Close-up of the interaction with L1 shown as a ribbon and the remaining CDRs as wireframe. (c) Bonding interactions between the L1 loop of one Fab and its neighboring Fab. (d) Least-squares superposition of the Cα atoms of the Fv from the Fab of the h-5E5 mAb with molecule II of the murine scFv (including the observed position of the APGST*AP ligand in molecule II), with the heavy- and light-chain amino-acid residues that bind the ligand labeled and shown using the stick representation in PyMOL, and with the remainder of both Fvs shown as cartoon shadows. It is apparent that changes in heavy–light chain domain association have led to significant differences in the relative positions of corresponding antigen-binding residues to the extent that the binding of antigen would be expected to be affected. H-5E5, white; scFv-5E5 heavy chain, light brown; scFv-5E5 light chain, light blue. The hydrogen bonds between the ligand and mouse scFv-5E5 are shown as dashed lines. CDRs are labeled. H1, red; H2, orange; H3, yellow; L1, green; L2, blue; L3, purple. Water molecules, gray. |
![[Figure 1]](ag5055fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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