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Title
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Three-dimensional solution structure of the src homology 2 domain of c-abl.
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Authors
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M.Overduin,
C.B.Rios,
B.J.Mayer,
D.Baltimore,
D.Cowburn.
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Ref.
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Cell, 1992,
70,
697-704.
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PubMed id
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Abstract
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SH2 regions are protein motifs capable of binding target protein sequences that
contain a phosphotyrosine. The solution structure of the abl SH2 product, a
protein of 109 residues and 12.1 kd, has been determined by multidimensional
nuclear magnetic resonance spectroscopy. It is a compact spherical domain with a
pair of three-stranded antiparallel beta sheets and a C-terminal alpha helix
enclosing the hydrophobic core. Three arginines project from a short N-terminal
alpha helix and one beta sheet into the putative phosphotyrosine-binding site,
which lies on a face distal from the termini. Comparison with other SH2
sequences supports a common global fold and mode of phosphotyrosine binding for
this family.
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