1yh3
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Crystal structure of human CD38 extracellular domain
OverviewOverview
Human CD38 is a multifunctional protein involved in diverse functions. As, an enzyme, it is responsible for the synthesis of two Ca2+ messengers, cADPR and NAADP; as an antigen, it is involved in regulating cell, adhesion, differentiation, and proliferation. Besides, CD38 is a marker of, progression of HIV-1 infection and a negative prognostic marker of B-CLL., We have determined the crystal structure of the soluble extracellular, domain of human CD38 to 1.9 A resolution. The enzyme's overall topology is, similar to the related proteins CD157 and the Aplysia ADP-ribosyl cyclase, except with large structural changes at the two termini. The extended, positively charged N terminus has lateral associations with the other CD38, molecule in the crystallographic asymmetric unit. The analysis of the CD38, substrate binding models revealed two key residues that may be critical in, controlling CD38's multifunctionality of NAD hydrolysis, ADP-ribosyl, cyclase, and cADPR hydrolysis activities.
About this StructureAbout this Structure
1YH3 is a Single protein structure of sequence from Homo sapiens. Active as NAD(+) nucleosidase, with EC number 3.2.2.5 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of human CD38 extracellular domain., Liu Q, Kriksunov IA, Graeff R, Munshi C, Lee HC, Hao Q, Structure. 2005 Sep;13(9):1331-9. PMID:16154090
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