Figure 1 | Scientific Reports

Figure 1

From: The crystal structure of the regulatory domain of the human sodium-driven chloride/bicarbonate exchanger

Figure 1

Dimerization determinants of ntcNDCBE. (a) ntcNDCBE is a dimer with 2-fold symmetry. The core domain of ntcNDCBE contains CR1 (light blue), VR2 (grey) and CR2 (light green). The 58 unstructured residues from Lys173 to Lys232 in VR2 are not visible in the electron density. Monomer B is shown in dark red. (b) Zoomed in view of the dimerization β-sheet, around 90 ° rotation along the x-axis from (a). The backbone of the residues of the dimerization β-sheet is shown as sticks. Only the side-chain residues from monomer A are shown. Hydrogen bonds are represented with black dotted lines. (c) Sequence alignment of the human N-terminal cytoplasmic domain of NBCs and AEs. Residues involved in the dimerization motif of ntcNDCBE are colour coded as in (a). The residues not present in ntcNDCBE are coloured grey. (d) Size-exclusion chromatography of 1 mg of ntcNDCBE (orange) on a Superdex 200 10/300 GL (GE Healthcare). ntcNDCBE eluted at 14.2 mL, corresponding to a dimer with an apparent MW of 80.6 kDa compared with molecular weight standards (grey).

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