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Article: Structural basis for formation and hydrolysis of the calcium messenger cyclic ADP-ribose by human CD38

TitleStructural basis for formation and hydrolysis of the calcium messenger cyclic ADP-ribose by human CD38
Authors
Issue Date2007
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 2007, v. 282 n. 8, p. 5853-5861 How to Cite?
AbstractHuman CD38 is a multifunctional ectoenzyme responsible for catalyzing the conversions from nicotinamide adenine dinucleotide (NAD) to cyclic ADP-ribose (cADPR) and from cADPR to ADP-ribose (ADPR). Both cADPR and ADPR are calcium messengers that can mobilize intracellular stores and activate influx as well. In this study, we determined three crystal structures of the human CD38 enzymatic domain complexed with cADPR at 1.5-Å resolution, with its analog, cyclic GDP-ribose (cGDPR) (1.68 Å) and with NGD (2.1 Å), a substrate analog of NAD. The results indicate that the binding of cADPR or cGDPR to the active site induces structural rearrangements in the dipeptide Glu 146-Asp147 by as much as 2.7 Å, providing the first direct evidence of a conformational change at the active site during catalysis. In addition, Glu226 is shown to be critical not only in catalysis but also in positioning of cADPR at the catalytic site through strong hydrogen bonding interactions. Structural details obtained from these complexes provide a step-by-step description of the catalytic processes in the synthesis and hydrolysis of cADPR. © 2007 by The American Society for Biochemistry and Molecular Biology, Inc.
Persistent Identifierhttp://hdl.handle.net/10722/91940
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLiu, Qen_HK
dc.contributor.authorKriksunov, IAen_HK
dc.contributor.authorGraeff, Ren_HK
dc.contributor.authorHon, CLen_HK
dc.contributor.authorHao, Qen_HK
dc.date.accessioned2010-09-17T10:31:09Z-
dc.date.available2010-09-17T10:31:09Z-
dc.date.issued2007en_HK
dc.identifier.citationJournal Of Biological Chemistry, 2007, v. 282 n. 8, p. 5853-5861en_HK
dc.identifier.issn0021-9258en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91940-
dc.description.abstractHuman CD38 is a multifunctional ectoenzyme responsible for catalyzing the conversions from nicotinamide adenine dinucleotide (NAD) to cyclic ADP-ribose (cADPR) and from cADPR to ADP-ribose (ADPR). Both cADPR and ADPR are calcium messengers that can mobilize intracellular stores and activate influx as well. In this study, we determined three crystal structures of the human CD38 enzymatic domain complexed with cADPR at 1.5-Å resolution, with its analog, cyclic GDP-ribose (cGDPR) (1.68 Å) and with NGD (2.1 Å), a substrate analog of NAD. The results indicate that the binding of cADPR or cGDPR to the active site induces structural rearrangements in the dipeptide Glu 146-Asp147 by as much as 2.7 Å, providing the first direct evidence of a conformational change at the active site during catalysis. In addition, Glu226 is shown to be critical not only in catalysis but also in positioning of cADPR at the catalytic site through strong hydrogen bonding interactions. Structural details obtained from these complexes provide a step-by-step description of the catalytic processes in the synthesis and hydrolysis of cADPR. © 2007 by The American Society for Biochemistry and Molecular Biology, Inc.en_HK
dc.languageengen_HK
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_HK
dc.relation.ispartofJournal of Biological Chemistryen_HK
dc.titleStructural basis for formation and hydrolysis of the calcium messenger cyclic ADP-ribose by human CD38en_HK
dc.typeArticleen_HK
dc.identifier.emailGraeff, R: graeffr@hku.hken_HK
dc.identifier.emailHon, CL: leehc@hku.hken_HK
dc.identifier.emailHao, Q: qhao@hku.hken_HK
dc.identifier.authorityGraeff, R=rp01464en_HK
dc.identifier.authorityHon, CL=rp00545en_HK
dc.identifier.authorityHao, Q=rp01332en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1074/jbc.M609093200en_HK
dc.identifier.pmid17182614-
dc.identifier.scopuseid_2-s2.0-34047231298en_HK
dc.identifier.hkuros134504-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-34047231298&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume282en_HK
dc.identifier.issue8en_HK
dc.identifier.spage5853en_HK
dc.identifier.epage5861en_HK
dc.identifier.eissn1083-351X-
dc.identifier.isiWOS:000244482300081-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridLiu, Q=35215401600en_HK
dc.identifier.scopusauthoridKriksunov, IA=6507909504en_HK
dc.identifier.scopusauthoridGraeff, R=7003614053en_HK
dc.identifier.scopusauthoridHon, CL=26642959100en_HK
dc.identifier.scopusauthoridHao, Q=7102508868en_HK

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