Figure 5.

Working molecular model of CGRP phenylalaninamide interaction with CLR residues L24 and L34. Energy minimized models for CGRP amino acids 32–37 (NH₂-VGSKAF-CONH₂) and CLR amino acids 23–35 (NH₂-ELEESPEDSIQLG-COOH) were performed as described in the "Methods". Hydrophobic interactions of CLR L24 and L34 with CGRP F37 and RAMP1 (not shown) cooperatively contributes to formation of the high affinity binding pocket essential for docking the C-terminal phenylalaninamide of the neuropeptide with the mature CGRP receptor heterodimer.