Kristelly Romana, Earnest Brett T, Krishnamoorthy Lakshmipriya, Tesmer John J G
Department of Chemistry and Biochemistry, The University of Texas at Austin, Austin, TX 78712, USA.
Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1859-62. doi: 10.1107/s0907444903018067. Epub 2003 Sep 19.
Leukemia-associated RhoGEF (LARG) is a multidomain protein that relays signals from Galpha(12/13)-coupled heptahelical receptors to GTPases that regulate the cytoskeleton. To understand the molecular basis of LARG-mediated signal transduction, structural analysis of its DH/PH domains has been initiated. The LARG DH/PH domains have been overexpressed in Escherichia coli as a TEV protease-cleavable fusion protein containing maltose-binding protein and a hexahistidine tag at the N- and C-termini, respectively. Crystals of the DH/PH domains were obtained (space group C2; unit-cell parameters a = 195.5, b = 46.0, c = 75.1 A, beta = 105.0 degrees ) and xenon and NaBr derivatives were generated which should allow the structure to be determined by MIRAS.
