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Figure 1 | Molecular Pain

Figure 1

From: CRMP-2 peptide mediated decrease of high and low voltage-activated calcium channels, attenuation of nociceptor excitability, and anti-nociception in a model of AIDS therapy-induced painful peripheral neuropathy

Figure 1

Scanning mutagenesis of CBD3 identifies better Ca2+ channel binding derivative peptides. (A) Superimposed ribbon overlaid on top of surface representations of the three-dimensional structure of the CRMP-2 monomer (RCSB databank PDB code: 2GSE) [79]. The location of the 6 amino acids of the CBD3 peptide are illustrated in the boxed region. (B) Ribbon representation of the helix harboring the first 6 amino acids (yellow; denoted in single letter code) of CBD3. (C) Matrix representation of normalized binding of CaV2.2 to CRMP-2 peptides singly mutated in silico to the indicated amino acids (italicized boldface font). The matrix was generated by Matrix2png [79]. Three peptides with mutations at position 6 (A6K), 9 (R9L) and 14 (G14F) displayed the highest binding to CaV2.2

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Molecular Pain

ISSN: 1744-8069

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