Catalysis associated conformational changes revealed by human cd38 complexed with a non-hydrolyzable substrate analog

Catalysis-associated Conformational Changes Revealed by Human CD38 Complexed with a Non-hydrolyzable Substrate Analog

Cyclic ADP-ribose hydrolase 1, cADPr hydrolase 1, Lymphocyte differentiation antigen CD38, T10, Acute lymphoblastic leukemia cells antigen CD38

KREAEARWRQTWSGPGTTKRFPETVLARCVKYTEIHPEMRHVDCQSVWDAFKGAFISKHPCDITEEDYQPLMKLGTQTVP
CNKILLWSRIKDLAHQFTQVQRDMFTLEDTLLGYLADDLTWCGEFDTSKINYQSCPDWRKDCSNNPVSVFWKTVSRRFAE
AACDVVHVMLDGSRSKIFDKDSTFGSVEVHNLQPEKVQTLEAWVIHGGREDSRDLCQDPTIKELESIISKRNIQFSCKNI
YRPDKFLQCVKNPEDSSCTSEI

100 mM MES, pH 6.0, and 10% PEG 4000, VAPOR DIFFUSION, HANGING DROP, temperature 300K

Human CD38 E226Q mutant bound with N1-cIDPR

There are two biological units in the crystallographic asymmetric unit.

Wild-type CD38 bound with N1-cIDPR, the catalytic pocket, conformational changes of the active site, substrate analog binding, HYDROLASE

RWRQQWSGPGTTKRFPETVLARCVKYTEIHPEMRHVDCQSVWDAFKGAFISKHPCNITEEDYQPLMKLGTQTVPCNKILL
WSRIKDLAHQFTQVQRDMFTLEDTLLGYLADDLTWCGEFNTSKINYQSCPDWRKDCSNNPVSVFWKTVSRRFAEAACDVV
HVMLNGSRSKIFDKNSTFGSVEVHNLQPEKVQTLEAWVIHGGREDSRDLCQDPTIKELESIISKRNIQFSCKNIYRPDKF
LQCVKNPEDSSCTSEI