Identification of a mouse orthologue of the human ras-GAP-SH3-domain binding protein and structural confirmation that these proteins contain an RNA recognition motif
Kennedy, D.; Wood, S.A.; Ramsdale, T.; Tam, P.P.; Steiner, K.A.; Mattick, J.S.
Biomedical Peptides Proteins and Nucleic Acids Structure Synthesis and Biological Activity 2(3): 93-99
1996
ISSN/ISBN: 1353-8616 PMID: 9575347 Document Number: 6937
Human ras-GTPase-activating protein (GAP120) SH3-domain-binding protein (G3BP) has recently been identified on the basis of its specific binding to the GAP120 SH3 binding domain. Here we report the identification of a mouse G3BP cDNA and the confirmation by three dimensional modelling of an RNA recognition motif (RRM) in the encoded protein. Mouse G3BP also contains an RGG domain, an acid-rich amino acid domain, and several SH3 domain-binding consensus sequences, indicating that mammalian G3BPs represent a new family of signal transduction proteins which connect tyrosine kinase-linked receptors to cellular RNA metabolism.
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