Three-dimensional solution structure of the src homology 2 domain of c-abl.
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Overduin M, Rios CB, Mayer BJ, Baltimore D, Cowburn D
Three-dimensional solution structure of the src homology 2 domain of c-abl.
Cell. 1992 Aug 21;70(4):697-704.
- PubMed ID
- 1505033 [ View in PubMed]
- Abstract
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.