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 journalArticle

133 Citations (Scopus)

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 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
JournalCell
Volume70
Issue number4
DOIs
StatePublished - Aug 21 1992
Externally publishedYes

Fingerprint

Phosphotyrosine
src Homology Domains
Amino Acid Motifs
Proteins
Nuclear magnetic resonance spectroscopy
Arginine
Carrier Proteins
Magnetic Resonance Spectroscopy
Binding Sites

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology

Cite this

Three-dimensional solution structure of the src homology 2 domain of c-abl. / Overduin, Michael; Rios, Carlos B.; Mayer, Bruce J.; Baltimore, David; Cowburn, David.

In: Cell, Vol. 70, No. 4, 21.08.1992, p. 697-704.

Research output: Contribution to journalArticle

Overduin, Michael ; Rios, Carlos B. ; Mayer, Bruce J. ; Baltimore, David ; Cowburn, David. / Three-dimensional solution structure of the src homology 2 domain of c-abl. In: Cell. 1992 ; Vol. 70, No. 4. pp. 697-704.
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