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Figure 1 | BMC Pharmacology

Figure 1

From: Identification of specific calcitonin-like receptor residues important for calcitonin gene-related peptide high affinity binding

Figure 1

Postulated interactions of specific CGRP domains with the CLR-RAMP1 heterodimer. Co-expression of the CLR with RAMP1 forms a mature CGRP receptor on the cell membrane surface. The characteristically long extracellular domains of the CLR-RAMP heterodimer create a high affinity binding pocket important for docking the C-terminal phenylalaninamide of CGRP. This interaction presents the CGRP N-terminus domain, essential for biological activity, to a "classical" agonist binding pocket formed in part by the transmembrane α-helices of the CLR-RAMP1 heterodimer.

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