IndraLab

Statements

SOS1 binds GRB2 and PGR. 7 / 7
| 7
sparser
"Grb2 binds to the PR domain of Sos1 with a 2:1 stoichiometry."
22360309
sparser
"Structural basis of the binding of Grb2 to the PR domain of Sos1 as two independent monomers versus a homodimer."
22360309
sparser
"These salient observations indicate that the positive cooperativity associated with bivalent binding of Grb2 to the PR domain of Sos1 arises through both the formation of additional intermolecular contacts (favorable enthalpy) as well as burial of additional hydrophobic surfaces (favorable entropy)."
22360309
sparser
"To understand stoichiometry and the underlying thermodynamic forces driving the formation of Grb2-Sos1 signaling complex, we next measured the binding of full-length Grb2 to the PR domain of Sos1 using ITC (representative data are shown in xref and all data summarized in xref )."
22360309
sparser
"Simply put, these observations strongly argue that the Grb2 homodimer bound to PR domain of Sos1 is structurally more stable than Grb2 monomers."
22360309
sparser
"MD simulations support the binding of Grb2 to the PR domain of Sos1 as a homodimer in lieu of two independent monomers."
22360309
sparser
"In light of these observations, it is thus conceivable that Grb2 could bind to the PR domain of Sos1 either as two independent monomers (Grb2-PR-Grb2), or alternatively as a homodimer ([Grb2] 2 -PR)."
22360309