Abstract
The adaptor molecule, Cbl, is involved as a negative regulator in a number of cell signaling pathways. Among its targets are cell surface receptors such as that for epidermal growth factor, and the protein tyrosine kinase ZAP-70. These interactions involve the binding of the N-terminal portion of Cbl to regions containing phosphorylated tyrosine residues. However there has been no indication from Cbl's sequence that it contained an SH2 domain the archetypal phospho-tyrosine binding motif. Consequently the recent structure of Cbl from Michael Eck's group (Meng, W., Sawasdikosol, S., Burakoff, S.J. & Eck, M.J.Nature, in the press) has come as something of a surprise.
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