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Article: Structure and enzymatic functions of human CD38

TitleStructure and enzymatic functions of human CD38
Authors
Issue Date2006
PublisherThe Feinstein Institute for Medical Research. The Journal's web site is located at http://www.molmed.org
Citation
Molecular Medicine, 2006, v. 12 n. 11-12, p. 317-323 How to Cite?
AbstractCD38 is a novel multifunctional protein that serves not only as an antigen but also as an enzyme. It catalyzes the metabolism of cyclic ADP-ribose and nicotinic acid adenine dinucleotide phosphate, two structurally and functionally distinct Ca2+ messengers targeting, respectively, the endoplasmic reticulum and lysosomal Ca2+ stores. The protein has recently been crystallized and its three-dimensional structure solved to a resolution of 1.9 Å. The crystal structure of a binary complex reveals critical interactions between residues at the active site and a bound substrate, providing mechanistic insights to its novel multi-functional catalysis. This article reviews the current advances in the understanding of the structural determinants that control the multiple enzymatic reactions catalyzed by CD38.
Persistent Identifierhttp://hdl.handle.net/10722/81347
ISSN
2015 Impact Factor: 3.53
2015 SCImago Journal Rankings: 2.372
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLee, HCen_HK
dc.date.accessioned2010-09-06T08:16:36Z-
dc.date.available2010-09-06T08:16:36Z-
dc.date.issued2006en_HK
dc.identifier.citationMolecular Medicine, 2006, v. 12 n. 11-12, p. 317-323en_HK
dc.identifier.issn1076-1551en_HK
dc.identifier.urihttp://hdl.handle.net/10722/81347-
dc.description.abstractCD38 is a novel multifunctional protein that serves not only as an antigen but also as an enzyme. It catalyzes the metabolism of cyclic ADP-ribose and nicotinic acid adenine dinucleotide phosphate, two structurally and functionally distinct Ca2+ messengers targeting, respectively, the endoplasmic reticulum and lysosomal Ca2+ stores. The protein has recently been crystallized and its three-dimensional structure solved to a resolution of 1.9 Å. The crystal structure of a binary complex reveals critical interactions between residues at the active site and a bound substrate, providing mechanistic insights to its novel multi-functional catalysis. This article reviews the current advances in the understanding of the structural determinants that control the multiple enzymatic reactions catalyzed by CD38.en_HK
dc.languageengen_HK
dc.publisherThe Feinstein Institute for Medical Research. The Journal's web site is located at http://www.molmed.orgen_HK
dc.relation.ispartofMolecular Medicineen_HK
dc.titleStructure and enzymatic functions of human CD38en_HK
dc.typeArticleen_HK
dc.identifier.emailLee, HC: leehc@hku.hken_HK
dc.identifier.authorityLee, HC=rp00545en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.2119/2006-00086.Leeen_HK
dc.identifier.pmid17380198-
dc.identifier.scopuseid_2-s2.0-33947623627en_HK
dc.identifier.hkuros134501en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33947623627&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume12en_HK
dc.identifier.issue11-12en_HK
dc.identifier.spage317en_HK
dc.identifier.epage323en_HK
dc.identifier.isiWOS:000245304600008-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridLee, HC=26642959100en_HK

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