1ab2
From Proteopedia
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| Activity: | Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE SRC HOMOLOGY 2 DOMAIN OF C-ABL
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Leukemia, Philadelphia chromosome-positive, resistant to imatinib OMIM:[189980]
About this Structure
1AB2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 09:55:16 2008
