Figure 5. The K372-E380 contact is required for GMPPNP-dependent stable dimer formation. The purified cytoplasmic domains of the indicated ATL2 variants (30 µM) were incubated with no nucleotide (−), 5 mM GDP, or 2 mM GMPPNP for 30 min at RT. Thereafter, samples were resolved on a Superdex 200 column. The Coomassie-stained proteins (∼60 kD) present in monomer (∼70 kD) and dimer peak (∼150 kD) positions from each column run are shown after SDS-PAGE. Also shown is a surface rendering of pre- and postfusion dimer conformers with K372 and E380 highlighted in blue and red, respectively. Models were drawn in PyMOL from Protein Data Bank no. 3QOF and 3QNU.
Figure 5.

The K372-E380 contact is required for GMPPNP-dependent stable dimer formation. The purified cytoplasmic domains of the indicated ATL2 variants (30 µM) were incubated with no nucleotide (−), 5 mM GDP, or 2 mM GMPPNP for 30 min at RT. Thereafter, samples were resolved on a Superdex 200 column. The Coomassie-stained proteins (∼60 kD) present in monomer (∼70 kD) and dimer peak (∼150 kD) positions from each column run are shown after SDS-PAGE. Also shown is a surface rendering of pre- and postfusion dimer conformers with K372 and E380 highlighted in blue and red, respectively. Models were drawn in PyMOL from Protein Data Bank no. 3QOF and 3QNU.

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