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1ab2
From Proteopedia
THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE SRC HOMOLOGY 2 DOMAIN OF C-ABL
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.
Three-dimensional solution structure of the src homology 2 domain of c-abl., Overduin M, Rios CB, Mayer BJ, Baltimore D, Cowburn D, Cell. 1992 Aug 21;70(4):697-704. PMID:1505033
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1AB2 is a 1 chain structure of sequence from Homo sapiens. Full experimental information is available from OCA.
Reference
- 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. PMID:1505033
Page seeded by OCA on Mon Feb 16 14:12:52 2009
