Fig. 5: Amino acid conservation mapped onto the structure of hMYDGF. | Nature Communications

Fig. 5: Amino acid conservation mapped onto the structure of hMYDGF.

From: Solution structure of human myeloid-derived growth factor suggests a conserved function in the endoplasmic reticulum

Fig. 5

a Using the ConSurf server, each residue of hMYDGF was binned from 1 (most variable, orange) to 9 (most conserved, blue) based on the alignment of 87 unique MYDGF protein homolog sequences (see Fig. 4) and mapped onto the structure of hMYDGF. In addition to the two cysteines that form the disulfide in the core of β-sandwich, the most conserved residues include, as highlighted in b, c, the C-terminus Glu-Leu sequence of the ERS and those in loops opposite the ERS. d A cavity (red) lined with conserved, hydrophobic residues (sticks; color-coded by conservation) beneath the surface shown in c was identified by CASTp and recreated in PyMOL as displayed here. The cavity has an average volume of 37 Å3 among the 20 most energetically stable conformers that represent the structure of hMYDGF.

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