Fig. 2: InlB321 site-specifically labeled variants in two possible MET:InlB dimer structures differing by the orientation of the MET:InlB monomers (MET in gray and InlB in blue). | Nature Communications

Fig. 2: InlB321 site-specifically labeled variants in two possible MET:InlB dimer structures differing by the orientation of the MET:InlB monomers (MET in gray and InlB in blue).

From: Single-molecule imaging and molecular dynamics simulations reveal early activation of the MET receptor in cells

Fig. 2

A Two InlB variants, K64C (H variant, mutation site highlighted in orange) and K280C (T variant, mutation site highlighted in green), are labeled with donor and acceptor fluorophores for single-molecule FRET. The protein structure is adapted from PDB 1H6T. B Form I assembly of (MET741:InlB321)2 dimer. Donor-acceptor distances between various combinations of two InlB variants were determined by AV simulations, yielding 7.6 nm (H-H), 7.6 nm (T-T), and 7.1 nm (T-H/H-T). The protein structure is adapted from PDB 2UZX. C Form II assembly of (MET741:InlB321)2 dimer. Donor-acceptor distances between two InlB variants were determined by AV simulations, yielding 12.2 nm (H-H), 5.9 nm (T-T), and 6.0 nm (T-H/H-T). The protein structure is adapted from PDB 2UZY.

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