Fig. 1: Structural homology of LCDV1-VILP with insulin and IGFs.
From: Interaction of a viral insulin-like peptide with the IGF-1 receptor produces a natural antagonist
a Sequence alignment of LCDV1-VILP with the human insulin and IGF-1. Strictly conserved cysteine residues are in red. The yellow square represents the C-domain, while the A- and the B-domains are in blue and green respectively. Cleavage sites composed of dibasic residues are underlined. Conserved amino acids are represented by an asterisk (*), and conservatively substituted residues are noted as a dot (.). b The LCDV1-VILP sequence was aligned with the 10 sequences showing the highest sequence identity. c Three-dimensional representation of insulin (PDB: 3I40), IGF-1 (AlphaFold2 prediction, pLDDT 78.23) and LCDV1-VILP as a single- (sc) and double chain (dc) molecules (AlphaFold2 predictions, pLDDT scores: scLCDV1 = 71.47, dcLCDV1 = 80.58). The A- and B-chains are represented in blue and green, respectively, and the C-peptide is in yellow. Residues involved in binding to site 1 and site 2 of the insulin/IGF-1 receptor are respectively in red and blue. The percentage of conserved binding residues with the sites 1 and 2 are indicated in red and blue, respectively.
