Skip to main content
. Author manuscript; available in PMC: 2011 Aug 1.
Published in final edited form as: Nat Struct Mol Biol. 2011 Jan 9;18(2):128–134. doi: 10.1038/nsmb.1967

Figure 4. Positioning hexahistidine tags to direct receptor binding.

Figure 4

(a) Secondary structure of the H-head domain beginning at cysteine 154 and ending with the last residue of the ectodomain. Hexahistidine tag insertion sites are indicated with numbered yellow circles. The unstructured final 10 amino acids of the H ectodomain to which the hexahistidine is linked in mutant 9 are indicated with an interrupted line. The amino acid residue preceding the insertion site of each tag is indicated above panel c. (b) Front view of the H-dimer head domain with the residues preceding and following each hexahistidine insertion site shown in yellow. The footprints of the receptors are indicated: red, SLAM-specific residues; blue, CD46-specific residues and purple, EpR-specific residues. (c) Protein expression analysis and dimerization capacity of the hexahistidine tag insertion mutants (top). On the top of panel c, the residue of insertion and the number of each hexahistidine tag are indicated. H-WT: non-mutated H-protein. Molecular weight markers are indicated on the left. β-actin expression levels were used as loading controls (bottom).