Three-dimensional solution structure of the src homology 2 domain of c-abl

Michael Overduin, Carlos B. Rios, Bruce J. Mayer, David Baltimore, David Cowburn

Research output: Contribution to journalArticlepeer-review

162 Scopus citations


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 β sheets and a C-terminal α helix enclosing the hydrophobic core. Three arginines project from a short N-terminal α helix and one β 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.

Original languageEnglish (US)
Pages (from-to)697-704
Number of pages8
Issue number4
StatePublished - Aug 21 1992
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)


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