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Cluster of Differentiation CD38

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[[Image:3gc6a.jpg|left|200px|thumb|Crystal Structure of bovine Cluster of Differentiation 38 (CD38) [[3gc6]]]]
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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]]'>
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{{STRUCTURE_3gc6| PDB=3gc6 | SIZE=300| SCENE=Cluster_of_Differentiation_38/Cv/1 |right|CAPTION=Cluster of Differentiation 38 (CD38) [[3gc6]] }}
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[[Cluster of Differentiation 38]] (CD38) 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++ signaling. The images at the left and at the right correspond to one representative CD38, ''i.e.'' the crystal structure of bovine Cluster of Differentiation 38 ([[3gc6]]).
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__TOC__
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{{TOC limit|limit=2}}
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== 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).<ref>PMID:16154090</ref>
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== Relevance ==
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CD38 is used as a marker for cell activation and for leukemia.
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== Structural highlights ==
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<scene name='42/422415/Cv/4'>CD38 active site contains NAD</scene>.<ref>PMID:16951430</ref>
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</StructureSection>
== 3D Structures of Cluster of Differentiation 38 ==
== 3D Structures of Cluster of Differentiation 38 ==
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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{{#tree:id=OrganizedByTopic|openlevels=0|
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* CD38
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**[[3gc6]] – bCD38 - bovine<br />
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**[[3gh3]], [[3ghh]] – bCD38 residues 32-278<br />
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**[[2eg9]] - CD38 enzymatic domain (mutant) – mouse<br />
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**[[2ef1]] - hCD38 enzymatic domain – human<br />
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**[[1yh3]] - hCD38 enzymatic domain (mutant)<br />
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**[[1zvm]] - hCD38 (mutant)<br />
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**[[1isf]] – hADPRC2 (mutant) <br />
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* CD38+ligand
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**[[3i9m]], [[3i9n]] – hCD38 enzymatic domain+ADPR analog<br />
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**[[3f6y]] – hCD38 enzymatic domain+Ca++<br />
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**[[3dzf]] - hCD38 enzymatic domain+intermediate<br />
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**[[3dzg]] - hCD38 enzymatic domain (mutant)+intermediate/nicotinamide complex<br />
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**[[3dzh]] - hCD38 enzymatic domain (mutant)+GTP<br />
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**[[3dzi]] - hCD38 enzymatic domain (mutant)+intermediate/GTP complex<br />
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**[[3dzj]], [[3dzk]] - hCD38 enzymatic domain (mutant)+NMN complex<br />
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**[[2pgj]], [[2pgl]] - hCD38 enzymatic domain (mutant)+substrate analog<br />
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**[[2o3t]] - hCD38 enzymatic domain (mutant)+cGDPR<br />
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**[[3u4h]], [[3u4i]] - hCD38 enzymatic domain (mutant)+cIDPR<br />
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**[[2o3u]] - hCD38 enzymatic domain (mutant)+NGD <br />
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**[[2o3q]], [[2o3r]], [[2o3s]] - hCD38 enzymatic domain (mutant)+cADPR<br />
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**[[4f45]] - hCD38 enzymatic domain (mutant)+ NAADP<br />
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**[[4f46]] - hCD38 enzymatic domain (mutant)+ NAADP + ADPRP<br />
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**[[4cmh]] - hCD38 enzymatic domain + antibody<br />
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**[[2i65]] – hCD38+NAD<br />
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**[[3kou]] - hCD38+NAD derivative<br />
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**[[2i67]] - hCD38 (mutant)+ADPR<br />
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**[[2hct]] - hCD38 enzymatic domain (mutant)+NMN<br />
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**[[3ofs]] - hCD38 enzymatic domain (mutant)+ ARA-2 F-ADPR<br />
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**[[3raj]] - hCD38 enzymatic domain (mutant)+ FAB<br />
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**[[3rok]], [[3rom]] - hCD38 (mutant) + arabinitol derivative<br />
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**[[3roq]] - hCD38 (mutant) + hydrofuran derivative<br />
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**[[3rop]] - hCD38 (mutant) + arabinitol derivative + nicotinamide<br />
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**[[3p5s]] - bADPRC + arabinitol derivative<br />
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=== CD38 ===
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*ADPRC
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**[[1r12]] - AcADPRC - ''Aplysia californica''<br />
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**[[1r0s]] – AcADPRC (mutant) <br />
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[[3gc6]] – bCD38 - bovine<br />
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*ADPRC+ligand
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[[3gh3]], [[3ghh]] – bCD38 residues 32-278<br />
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[[2eg9]] - CD38 enzymatic domain (mutant) – mouse<br />
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[[2ef1]] - hCD38 enzymatic domain – human<br />
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[[1yh3]] - hCD38 enzymatic domain (mutant)<br />
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[[1zvm]] - hCD38 (mutant)<br />
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**[[1r15]] - AcADPRC+nicotinamide<br />
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**[[3i9j]] – AcADPRC+nicotinamide+2F-NAD+2F-ADPRI<br />
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**[[3i9k]] – AcADPRC (mutant)+NAD<br />
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**[[3i9l]] – AcADPRC (mutant)+N1-CIDPR<br />
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**[[3i9o]] – AcADPRC+Ribosyl-2F-ADPR<br />
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**[[3zwx]], [[3zwy]] – AcADPRC + 8-Br-ADPR<br />
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**[[1r16]] - AcADPRC+3-pyridinylcarbinol<br />
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**[[3zwm]] – AcADPRC + NAD + cADPR<br />
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**[[3zwn]] – AcADPRC + NGD + cGDPR<br />
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**[[3zwo]] – AcADPRC + NGD + GDPR<br />
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**[[3zwp]], [[3zwv]], [[3zww]] – AcADPRC+ diphosphate ribosyl ara-2F-ADPR<br />
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=== CD38+ligand ===
 
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}}
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== References ==
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<references/>
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[[3i9m]], [[3i9n]] – hCD38 enzymatic domain+ADPR analog<br />
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[[Category:Topic Page]]
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[[3f6y]] – hCD38 enzymatic domain+Ca++<br />
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[[3dzf]] - hCD38 enzymatic domain+intermediate<br />
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[[3dzg]] - hCD38 enzymatic domain (mutant)+intermediate/nicotinamide complex<br />
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[[3dzh]] - hCD38 enzymatic domain (mutant)+GTP<br />
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[[3dzi]] - hCD38 enzymatic domain (mutant)+intermediate/GTP complex<br />
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[[3dzj]], [[3dzk]] - hCD38 enzymatic domain (mutant)+NMN complex<br />
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[[2pgj]], [[2pgl]] - hCD38 enzymatic domain (mutant)+substrate analog<br />
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[[2o3t]] - hCD38 enzymatic domain (mutant)+cGDPR<br />
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[[2o3u]] - hCD38 enzymatic domain (mutant)+NGD <br />
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[[2o3q]], [[2o3r]], [[2o3s]] - hCD38 enzymatic domain (mutant)+cADPR<br />
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[[2i65]] – hCD38+NAD<br />
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[[2i66]] - hCD38 (mutant)+GDP intermediate<br />
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[[2i67]] - hCD38 (mutant)+ADPR<br />
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[[2hct]] - hCD38 enzymatic domain (mutant)+NMN<br />
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Current revision

Human Cluster of Differentiation 38 (CD38) complex with NAD 2i65

Drag the structure with the mouse to rotate

3D Structures of Cluster of Differentiation 38

Updated on 10-July-2018

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
  2. 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

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Michal Harel, Alexander Berchansky, Jaime Prilusky

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