Figure 1From: A single amino acid change within the R2 domain of the VvMYB5b transcription factor modulates affinity for protein partners and target promoters selectivityStructure of the R2R3 domain of different MYB proteins. (A) Protein sequence alignment of the R2R3 domain of grapevine MYB transcription factors regulating the flavonoid pathway and mouse (Mus musculus) c-MYB. GenBank accession numbers are indicated below: VvMYB5b (AY899404), VvMYB5a (AY555190), VvMYBPA1 (AM259485), VvMYBA1 (AB097923), and Mmc-MYB (NP_034978). Identical residues are shown in white on a red background, and conserved residues are red. The R/L mutation is indicated with a dark triangle, residues interacting with DNA bases [30, 35] are indicated with either a dark square or an asterisk for strong and weak interactions respectively. Dark circles denote residues interacting with bHLH partners [24]. Diamonds denote residues involved in the hydrophobic pocket in domain R2 and amino acids involved in salt bridge interactions in Mmc-MYB [30] are highlighted with red arrow heads. This figure was drawn using web ESPript [61]. (B) R2 and R3 domains of the VvMyb5b modeled structure obtained deduced from the X-ray diffraction structure of the mouse c-MYB proto-oncogene R2-R3 domain (pdb entry code 1gv2). The figure was drawn with PyMOL [62]. (C) Stereo view of the environment of residue R69 within the R2 domain.Back to article page