Cluster of Differentiation CD38: Difference between revisions
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<StructureSection load='2i65' size='450' side='right' scene='42/422415/Cv/3' caption='Human Cluster of Differentiation 38 (CD38) complex with NAD [[2i65]]'> | <StructureSection load='2i65' size='450' side='right' scene='42/422415/Cv/3' caption='Human Cluster of Differentiation 38 (CD38) complex with NAD [[2i65]]'> | ||
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== Function == | == Function == | ||
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<scene name='42/422415/Cv/4'>CD38 active site contains NAD</scene>.<ref>PMID:16951430</ref> | <scene name='42/422415/Cv/4'>CD38 active site contains NAD</scene>.<ref>PMID:16951430</ref> | ||
</StructureSection> | </StructureSection> | ||
== 3D Structures of Cluster of Differentiation 38 == | == 3D Structures of Cluster of Differentiation 38 == | ||
Latest revision as of 16:16, 10 July 2018
FunctionCluster of Differentiation 38 (CD38), known also as ADP-ribosyl cyclase 1 (ADPRC1), catalyzes the synthesis and hydrolysis of cyclic ADP-ribose from NAD+ to ADP-ribose (ADPR). It is found on the surface of immune cells. It also functions in cell adhesion, signal transduction and Ca+2 signaling. ADP-ribosyl cyclase (ADPRC) is the Aplysia californica homolog of CD38. It catalyzes the synthesis and hydrolysis of cyclic ADP-ribose. It uses NAD+ as substrate and produces cyclic ADP-ribose (cADPR).[1] RelevanceCD38 is used as a marker for cell activation and for leukemia. Structural highlights.[2] |
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3D Structures of Cluster of Differentiation 383D Structures of Cluster of Differentiation 38
Updated on 10-July-2018
ReferencesReferences
- ↑ Liu Q, Kriksunov IA, Graeff R, Munshi C, Lee HC, Hao Q. Crystal structure of human CD38 extracellular domain. Structure. 2005 Sep;13(9):1331-9. PMID:16154090 doi:http://dx.doi.org/10.1016/j.str.2005.05.012
- ↑ Liu Q, Kriksunov IA, Graeff R, Munshi C, Lee HC, Hao Q. Structural basis for the mechanistic understanding of human CD38-controlled multiple catalysis. J Biol Chem. 2006 Oct 27;281(43):32861-9. Epub 2006 Sep 2. PMID:16951430 doi:10.1074/jbc.M606365200