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Cluster of Differentiation CD38

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== Function ==
== Function ==
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[[Cluster 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).
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[[Cluster 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).<ref>PMID:16154090</ref>
== Relevance ==
== Relevance ==
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== References ==
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<references/>
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[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 12:34, 24 November 2015

Glycosylated Cluster of Differentiation 38 (CD38) complex with sulfate 3gc6

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3D Structures of Cluster of Differentiation 38

Updated on 24-November-2015

References

  1. ↑ 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

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Michal Harel, Alexander Berchansky, Jaime Prilusky

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