Grb2 mediates the EGF-dependent activation of guanine nucleotide exchange on Ras

Article Abstract:

Overexpression of Grb2 increases guanine-nucleotide exchange rate by working up a complex with the ligand-activated receptor. This coupling regulates tyrosine kinase that modulates Ras activity and mitogen-activated protein kinase. The ability of Grb2 to enhance Ras activity by facilitating guanine-nucleotide exchange rate is observed as a conserved mechanism that developed to advance receptor signals to Ras. Translocation can bond receptor activation to undiminished exchange factor activity, by transporting the factor to the subcellular compartment.

Analysis, Protein binding, Epidermal growth factor, Epidermal growth factors, Nucleotides

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Structure of a heparin-linked biologically active dimer of fibroblast growth factor

Article Abstract:

The crystal structure of the biologically active, heparin-decasaccharide-linked dimer of oligomerize acidic fibroblast growth factors (aFGF) shows a unique mode of ligand-induced protein dimerization. This aFGF dimer is bridged by heparin and does not have a protein-protein interface. Linking crystallographic and mutagenesis makes it possible to develop a model for the dimerization of FGF receptors that may indicate how the FGF ligands transmit different forms of signal in many different cells expressing the various isoforms of FGF receptors.

Fibroblast growth factors

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The structural basis of the activation of Ras by Sos

Article Abstract:

Ras proteins are guanine-nucleotide-binding enzymes acting as molecular switches between active GTP-bound and inactive GDP-bound states. The crystal structure of human H-Ras complexed with the Son of sevenless (Sos) protein RAS guanine-nucleotide-exchange-factor region, has been determined. Sos disrupts the usually tight interaction of nucleotides with Ras, and the structure of Ras-Sos complex, indicates routes for the design of inhibitors to block the activation of Ras by Sos.

Observations, Proteins, Cell proliferation

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