Crystal Structure of the Mammalian Grb2 Adaptor
Copyright policy )Crystal Structure of the Mammalian Grb2 Adaptor
The mammalian growth factor receptor-binding protein Grb2 is an adaptor that mediates activation of guanine nucleotide exchange on Ras. Grb2 binds to the receptor through its SH2 domain and to the carboxyl-terminal domain of Son of sevenless through its two SH3 domains. It is thus a key element in the signal transduction pathway. The crystal structure of Grb2 was determined to 3.1 angstrom resolution. The asymmetric unit is composed of an embedded dimer. The interlaced junctions between the SH2 and SH3 domains bring the two adjacent faces of the SH3 domains in van der Waals contact but leave room for the binding of proline-rich peptides.
- Paris 13 University France
- University of Paris France
Models, Molecular, Binding Sites, Protein Conformation, Molecular Sequence Data, Proteins, Hydrogen Bonding, Crystallography, X-Ray, Protein Structure, Secondary, ErbB Receptors, Computer Graphics, Amino Acid Sequence, Crystallization, Adaptor Proteins, Signal Transducing, GRB2 Adaptor Protein
Models, Molecular, Binding Sites, Protein Conformation, Molecular Sequence Data, Proteins, Hydrogen Bonding, Crystallography, X-Ray, Protein Structure, Secondary, ErbB Receptors, Computer Graphics, Amino Acid Sequence, Crystallization, Adaptor Proteins, Signal Transducing, GRB2 Adaptor Protein
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