1AB2

THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE SRC HOMOLOGY 2 DOMAIN OF C-ABL

Summary for 1AB2

• Entry DOI: 10.2210/pdb1ab2/pdb
• Descriptor: C-ABL TYROSINE KINASE SH2 DOMAIN (1 entity in total)
• Functional Keywords: transferase(phosphotransferase)
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytoskeleton. Isoform IB: Nucleus membrane; Lipid-anchor: P00519
• Total number of polymer chains: 1
• Total formula weight: 12159.39

Authors

Overduin, M.,Rios, C.B.,Mayer, B.J.,Baltimore, D.,Cowburn, D. (deposition date: 1993-07-19, release date: 1994-01-31, Last modification date: 2024-05-22)

Primary citation

Overduin, M.,Rios, C.B.,Mayer, B.J.,Baltimore, D.,Cowburn, D.
Three-dimensional solution structure of the src homology 2 domain of c-abl.
Cell(Cambridge,Mass.), 70:697-704, 1992

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.

PubMed: 1505033
DOI: 10.1016/0092-8674(92)90437-H

Experimental method

SOLUTION NMR