Structural Characterization of a Therapeutic Anti-Methamphetamine Antibody Fragment: Oligomerization and Binding of Active Metabolites
Figure 2
A comparison of the free form of scfv6H4 with the METH bound form.
(a) A stereo-view depicting the superposition of the Cα atoms of the free form (pink) with the METH complex (purple). The largest deviations are all in the CDR loops. The METH is shown in green. The CDR H1, CDR H2 and CDR H3 are labeled as H1, H2 and H3. Likewise, CDR L1, CDR L2 and CDR L3 are labeled as L1, L2 and L3. Residues Gly H26, Asp H27, Ser H97 and Met H100B are labeled as 26, 27, 97 and 100B. The light chains are shown in lighter colors.
(b) Trimer formation. Left panel: A lateral of a view cartoon representation of the trimer. The three molecules assemble around the 3-fold axis to give it a light bulb-like shape. The Ni2+ ion is shown as a sphere (in the stem region on the top) and the sulfate moiety (towards the bottom of the sphere) is shown as a CPK model. Right panel: A view from the top along the 3-fold axis. The three molecules are labeled as Mol-A (red), Mol-B (green) and Mol-C (blue). The light chains are shown in lighter colors.