Dissecting the thermodynamics of GAP–RhoA interactions
F Jelen, P Lachowicz, W Apostoluk, A Mateja… - Journal of structural …, 2009 - Elsevier
We describe a detailed study of the RhoA-binding epitope of the GAP domain of Graf,
including the determination of the thermodynamic and kinetic parameters of the interaction
of wild-type domain, and of its 15 single-site mutants, with cognate GTPases. We show that
residues important for the structural integrity of the Arg-finger loop are critical for binding Rho
and for the catalytic activity of GAP, but GTPase selectivity appears to be modulated by a
much more subtle interplay of electrostatic and hydrophobic interactions involving residues …
including the determination of the thermodynamic and kinetic parameters of the interaction
of wild-type domain, and of its 15 single-site mutants, with cognate GTPases. We show that
residues important for the structural integrity of the Arg-finger loop are critical for binding Rho
and for the catalytic activity of GAP, but GTPase selectivity appears to be modulated by a
much more subtle interplay of electrostatic and hydrophobic interactions involving residues …
