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Article: Crystal structure of Aplysia ADP ribosyl cyclase, a homologue of the bifunctional ectozyme CD38

TitleCrystal structure of Aplysia ADP ribosyl cyclase, a homologue of the bifunctional ectozyme CD38
Authors
Prasad, GSMcree, DEStura, EALevitt, DGLee, HCStout, CD
Issue Date1996
Citation
Nature Structural Biology, 1996, v. 3 n. 11, p. 957-964 How to Cite?
DOI: http://dx.doi.org/10.1038/nsb1196-957
AbstractADP ribosyl cyclase synthesizes the novel secondary messenger cyclic ADP ribose (cADPR) utilizing NAD as a substrate. The enzyme shares extensive sequence similarity with two lymphocyte antigens, CD38 and BST-1, which hydrolyse as well as synthesize cADPR. The crystal structure provides a model for these cell surface enzymes. Cyclase contains two spatially separated pockets composed of sequence conserved residues, suggesting that the cyclization reaction may entail use of distinct sites. The enzyme dimer encloses a cavity which may entrap the intermediate, ADP ribose.
Persistent Identifierhttp://hdl.handle.net/10722/171627
ISSN
1072-8368
ISI Accession Number ID
WOS:A1996VT09300016
References
References in Scopus

 

DC FieldValueLanguage
dc.contributor.authorPrasad, GSen_US
dc.contributor.authorMcree, DEen_US
dc.contributor.authorStura, EAen_US
dc.contributor.authorLevitt, DGen_US
dc.contributor.authorLee, HCen_US
dc.contributor.authorStout, CDen_US
dc.date.accessioned2012-10-30T06:16:02Z-
dc.date.available2012-10-30T06:16:02Z-
dc.date.issued1996en_US
dc.identifier.citationNature Structural Biology, 1996, v. 3 n. 11, p. 957-964en_US
dc.identifier.issn1072-8368en_US
dc.identifier.urihttp://hdl.handle.net/10722/171627-
dc.description.abstractADP ribosyl cyclase synthesizes the novel secondary messenger cyclic ADP ribose (cADPR) utilizing NAD as a substrate. The enzyme shares extensive sequence similarity with two lymphocyte antigens, CD38 and BST-1, which hydrolyse as well as synthesize cADPR. The crystal structure provides a model for these cell surface enzymes. Cyclase contains two spatially separated pockets composed of sequence conserved residues, suggesting that the cyclization reaction may entail use of distinct sites. The enzyme dimer encloses a cavity which may entrap the intermediate, ADP ribose.en_US
dc.languageengen_US
dc.relation.ispartofNature Structural Biologyen_US
dc.subject.meshAdp-Ribosyl Cyclaseen_US
dc.subject.meshAdenosine Diphosphate Ribose - Metabolismen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAnimalsen_US
dc.subject.meshAntigens, Cden_US
dc.subject.meshAntigens, Cd38en_US
dc.subject.meshAntigens, Differentiation - Chemistryen_US
dc.subject.meshAplysia - Enzymologyen_US
dc.subject.meshConserved Sequenceen_US
dc.subject.meshCrystallography, X-Rayen_US
dc.subject.meshDimerizationen_US
dc.subject.meshGpi-Linked Proteinsen_US
dc.subject.meshMembrane Glycoproteins - Chemistryen_US
dc.subject.meshModels, Molecularen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshN-Glycosyl Hydrolases - Chemistryen_US
dc.subject.meshProtein Conformationen_US
dc.subject.meshSequence Homology, Amino Aciden_US
dc.titleCrystal structure of Aplysia ADP ribosyl cyclase, a homologue of the bifunctional ectozyme CD38en_US
dc.typeArticleen_US
dc.identifier.emailLee, HC:leehc@hku.hken_US
dc.identifier.authorityLee, HC=rp00545en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1038/nsb1196-957en_US
dc.identifier.pmid8901875-
dc.identifier.scopuseid_2-s2.0-0029858306en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0029858306&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume3en_US
dc.identifier.issue11en_US
dc.identifier.spage957en_US
dc.identifier.epage964en_US
dc.identifier.isiWOS:A1996VT09300016-
dc.identifier.scopusauthoridPrasad, GS=7201752888en_US
dc.identifier.scopusauthoridMcRee, DE=7006894969en_US
dc.identifier.scopusauthoridStura, EA=7006685217en_US
dc.identifier.scopusauthoridLevitt, DG=7102923276en_US
dc.identifier.scopusauthoridLee, HC=26642959100en_US
dc.identifier.scopusauthoridStout, CD=7102760401en_US
dc.identifier.issnl1072-8368-

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