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VEGFRs, like other RTKs, become activated when ligand receptor binding and resultant dimerization happen.
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The extracellular cysteine-rich domains of ErbB2 receptors play important roles in ligand binding and receptor dimerization.
EGF binding and receptor dimerization are assumed to interact mutually.
Examples include proteins involved in disulfide bonding, GTP binding and protein dimerization.
The first uses ATP binding and NBD dimerization as the pumping mechanism.
Antibody inhibitors block the extracellular ligand binding domain of EGFR thereby preventing ligand binding and receptor dimerization.
According to thermodynamic constraints [ 33, 28], EGF binding and receptor dimerization have to interact mutually fulfilling the Wegscheider conditions.
Dimerization is a molecular process such as ligand binding, and dimerization can influence or can be influenced by all other processes within the considered network.
The inserted sub-domain is shown to be involved in substrate binding and dimerization.
Open image in new window Figure 2 MABP-1 is an ATPase and the accessory domain of MABP-1 is vital for erythromycin binding and dimerization.
The N-terminal region of the receptors is involved in membrane localization, ethylene binding, and dimerization.
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