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 language | English (US) |
|---|---|
| Pages (from-to) | 697-704 |
| Number of pages | 8 |
| Journal | Cell |
| Volume | 70 |
| Issue number | 4 |
| DOIs | |
| State | Published - Aug 21 1992 |
| Externally published | Yes |
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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 journal › Article
}
TY - JOUR
T1 - Three-dimensional solution structure of the src homology 2 domain of c-abl
AU - Overduin, Michael
AU - Rios, Carlos B.
AU - Mayer, Bruce J.
AU - Baltimore, David
AU - Cowburn, David
PY - 1992/8/21
Y1 - 1992/8/21
N2 - 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.
AB - 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.
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U2 - 10.1016/0092-8674(92)90437-H
DO - 10.1016/0092-8674(92)90437-H
M3 - Article
C2 - 1505033
AN - SCOPUS:0026669472
VL - 70
SP - 697
EP - 704
JO - Cell
JF - Cell
SN - 0092-8674
IS - 4
ER -