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Article: Crystal structure of human CD38 extracellular domain

TitleCrystal structure of human CD38 extracellular domain
Authors
Liu, QKriksunov, IAGraeff, RMunshi, CHon, CLHao, Q
Issue Date2005
PublisherCell Press. The Journal's web site is located at http://www.elsevier.com/locate/str
Citation
Structure, 2005, v. 13 n. 9, p. 1331-1339 How to Cite?
DOI: http://dx.doi.org/10.1016/j.str.2005.05.012
AbstractHuman CD38 is a multifunctional protein involved in diverse functions. As an enzyme, it is responsible for the synthesis of two Ca2+ messengers, cADPR and NAADP; as an antigen, it is involved in regulating cell adhesion, differentiation, and proliferation. Besides, CD38 is a marker of progression of HIV-1 infection and a negative prognostic marker of B-CLL. We have determined the crystal structure of the soluble extracellular domain of human CD38 to 1.9 Å resolution. The enzyme's overall topology is similar to the related proteins CD157 and the Aplysia ADP-ribosyl cyclase, except with large structural changes at the two termini. The extended positively charged N terminus has lateral associations with the other CD38 molecule in the crystallographic asymmetric unit. The analysis of the CD38 substrate binding models revealed two key residues that may be critical in controlling CD38's multifunctionality of NAD hydrolysis, ADP-ribosyl cyclase, and cADPR hydrolysis activities. ©2005 Elsevier Ltd All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/91920
ISSN
0969-2126
2022 Impact Factor: 5.7
2020 SCImago Journal Rankings: 2.907
ISI Accession Number ID
WOS:000232119200014
References
References in Scopus

 

DC FieldValueLanguage
dc.contributor.authorLiu, Qen_HK
dc.contributor.authorKriksunov, IAen_HK
dc.contributor.authorGraeff, Ren_HK
dc.contributor.authorMunshi, Cen_HK
dc.contributor.authorHon, CLen_HK
dc.contributor.authorHao, Qen_HK
dc.date.accessioned2010-09-17T10:30:34Z-
dc.date.available2010-09-17T10:30:34Z-
dc.date.issued2005en_HK
dc.identifier.citationStructure, 2005, v. 13 n. 9, p. 1331-1339en_HK
dc.identifier.issn0969-2126en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91920-
dc.description.abstractHuman CD38 is a multifunctional protein involved in diverse functions. As an enzyme, it is responsible for the synthesis of two Ca2+ messengers, cADPR and NAADP; as an antigen, it is involved in regulating cell adhesion, differentiation, and proliferation. Besides, CD38 is a marker of progression of HIV-1 infection and a negative prognostic marker of B-CLL. We have determined the crystal structure of the soluble extracellular domain of human CD38 to 1.9 Å resolution. The enzyme's overall topology is similar to the related proteins CD157 and the Aplysia ADP-ribosyl cyclase, except with large structural changes at the two termini. The extended positively charged N terminus has lateral associations with the other CD38 molecule in the crystallographic asymmetric unit. The analysis of the CD38 substrate binding models revealed two key residues that may be critical in controlling CD38's multifunctionality of NAD hydrolysis, ADP-ribosyl cyclase, and cADPR hydrolysis activities. ©2005 Elsevier Ltd All rights reserved.en_HK
dc.languageengen_HK
dc.publisherCell Press. The Journal's web site is located at http://www.elsevier.com/locate/stren_HK
dc.relation.ispartofStructureen_HK
dc.titleCrystal structure of human CD38 extracellular domainen_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.doi10.1016/j.str.2005.05.012en_HK
dc.identifier.pmid16154090-
dc.identifier.scopuseid_2-s2.0-24344490302en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-24344490302&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume13en_HK
dc.identifier.issue9en_HK
dc.identifier.spage1331en_HK
dc.identifier.epage1339en_HK
dc.identifier.isiWOS:000232119200014-
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.scopusauthoridMunshi, C=7003972383en_HK
dc.identifier.scopusauthoridHon, CL=26642959100en_HK
dc.identifier.scopusauthoridHao, Q=7102508868en_HK
dc.identifier.issnl0969-2126-

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