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- Publisher Website: 10.1016/j.str.2005.05.012
- Scopus: eid_2-s2.0-24344490302
- PMID: 16154090
- WOS: WOS:000232119200014
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Article: Crystal structure of human CD38 extracellular domain
Title | Crystal structure of human CD38 extracellular domain |
---|---|
Authors | |
Issue Date | 2005 |
Publisher | Cell 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? |
Abstract | Human 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 Identifier | http://hdl.handle.net/10722/91920 |
ISSN | 2023 Impact Factor: 4.4 2023 SCImago Journal Rankings: 2.456 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Liu, Q | en_HK |
dc.contributor.author | Kriksunov, IA | en_HK |
dc.contributor.author | Graeff, R | en_HK |
dc.contributor.author | Munshi, C | en_HK |
dc.contributor.author | Hon, CL | en_HK |
dc.contributor.author | Hao, Q | en_HK |
dc.date.accessioned | 2010-09-17T10:30:34Z | - |
dc.date.available | 2010-09-17T10:30:34Z | - |
dc.date.issued | 2005 | en_HK |
dc.identifier.citation | Structure, 2005, v. 13 n. 9, p. 1331-1339 | en_HK |
dc.identifier.issn | 0969-2126 | en_HK |
dc.identifier.uri | http://hdl.handle.net/10722/91920 | - |
dc.description.abstract | Human 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.language | eng | en_HK |
dc.publisher | Cell Press. The Journal's web site is located at http://www.elsevier.com/locate/str | en_HK |
dc.relation.ispartof | Structure | en_HK |
dc.title | Crystal structure of human CD38 extracellular domain | en_HK |
dc.type | Article | en_HK |
dc.identifier.email | Graeff, R: graeffr@hku.hk | en_HK |
dc.identifier.email | Hon, CL: leehc@hku.hk | en_HK |
dc.identifier.email | Hao, Q: qhao@hku.hk | en_HK |
dc.identifier.authority | Graeff, R=rp01464 | en_HK |
dc.identifier.authority | Hon, CL=rp00545 | en_HK |
dc.identifier.authority | Hao, Q=rp01332 | en_HK |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1016/j.str.2005.05.012 | en_HK |
dc.identifier.pmid | 16154090 | - |
dc.identifier.scopus | eid_2-s2.0-24344490302 | en_HK |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-24344490302&selection=ref&src=s&origin=recordpage | en_HK |
dc.identifier.volume | 13 | en_HK |
dc.identifier.issue | 9 | en_HK |
dc.identifier.spage | 1331 | en_HK |
dc.identifier.epage | 1339 | en_HK |
dc.identifier.isi | WOS:000232119200014 | - |
dc.publisher.place | United States | en_HK |
dc.identifier.scopusauthorid | Liu, Q=35215401600 | en_HK |
dc.identifier.scopusauthorid | Kriksunov, IA=6507909504 | en_HK |
dc.identifier.scopusauthorid | Graeff, R=7003614053 | en_HK |
dc.identifier.scopusauthorid | Munshi, C=7003972383 | en_HK |
dc.identifier.scopusauthorid | Hon, CL=26642959100 | en_HK |
dc.identifier.scopusauthorid | Hao, Q=7102508868 | en_HK |
dc.identifier.issnl | 0969-2126 | - |