Fig. 1: Solution structure of hMYDGF solved by protein NMR at pH 6. | Nature Communications

Fig. 1: Solution structure of hMYDGF solved by protein NMR at pH 6.

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

Fig. 1

a The lowest pseudo-potential energy NMR conformer of hMYDGF. The structure is made up of ten β-strands (β1–β10) that constitute three β-sheets (red, orange, green), a short α-helix (blue), and a disulfide bridge between strands β3 and β5 (right image, stick representation). The first five N-terminal residues were introduced as a result of cloning (black) and the last four C-terminal residues (RTEL) comprise the ERS (yellow). b Diagram of the β-strand connectivity colored by β-sheet with the disulfide linkage displayed as a dotted line. c Surface charge distribution of hMYDGF (lacking cloning residues) calculated at pH 6 depicting positively charged (blue), negatively charged (red), and uncharged (white) regions scattered across the protein. d Overlay of the 20 most energetically stable hMYDGF conformers presented in stereo view. Ordered hMYDGF residues align with an RMSD of 0.72 Å for backbone heavy atoms (Table 1), with the highest degree of flexibility at the N-terminus (black), the C-terminus (yellow), and the loop between β7 and the α-helix (gray).

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