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Article: Solution structure of the C-terminal domain of the ciliary neurotrophic factor (CNTF) receptor and ligand free associations among components of the CNTF receptor complex

TitleSolution structure of the C-terminal domain of the ciliary neurotrophic factor (CNTF) receptor and ligand free associations among components of the CNTF receptor complex
Authors
Issue Date2003
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, 2003, v. 278 n. 26, p. 23285-23294 How to Cite?
AbstractThe functional receptor complex of ciliary neurotrophic factor (CNTF), a member of the gp130 family of cytokines, is composed of CNTF, the CNTF receptor a (CNTFR), gp130, and the leukemia inhibitory factor receptor (LIFR). However, the nature of the receptor-mediated interactions in this complex has not yet been resolved. To address this issue we have determined the solution structure of the C-terminal or BC domain of CNTFR and studied the interactions of CNTFR with LIFR and gp130. We reported previously that the membrane distal cytokine-binding domain (CBD1) of LIFR could interact in vitro with soluble CNTFR (sCNTFR) in the absence of CNTF. Here we show that the CBD of human gp130 can also bind in vitro to sCNTFR in the absence of CNTF. In addition, the gp130 CBD could compete with the LIFR CBD1 for the binding of sCNTFR. Substitution of residues in the gp130 CBD, the LIFR CBD1, and the CNTFR BC domain that are expected to be involved in receptor-receptor interactions significantly reduced their interactions. An NMR chemical shift perturbation study of the interaction between the BC domains of CNTFR and gp130 further mapped the interaction surface. These data suggest that both the gp130 CBD and the LIFR CBD1 interact with CNTFR in a similar way and provide insights into the nature of the CNTF receptor complex.
Persistent Identifierhttp://hdl.handle.net/10722/96915
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorMan, Den_HK
dc.contributor.authorHe, Wen_HK
dc.contributor.authorSze, KHen_HK
dc.contributor.authorGong, Ken_HK
dc.contributor.authorSmith, DKen_HK
dc.contributor.authorZhu, Gen_HK
dc.contributor.authorIp, NYen_HK
dc.date.accessioned2010-09-25T16:49:41Z-
dc.date.available2010-09-25T16:49:41Z-
dc.date.issued2003en_HK
dc.identifier.citationJournal Of Biological Chemistry, 2003, v. 278 n. 26, p. 23285-23294en_HK
dc.identifier.issn0021-9258en_HK
dc.identifier.urihttp://hdl.handle.net/10722/96915-
dc.description.abstractThe functional receptor complex of ciliary neurotrophic factor (CNTF), a member of the gp130 family of cytokines, is composed of CNTF, the CNTF receptor a (CNTFR), gp130, and the leukemia inhibitory factor receptor (LIFR). However, the nature of the receptor-mediated interactions in this complex has not yet been resolved. To address this issue we have determined the solution structure of the C-terminal or BC domain of CNTFR and studied the interactions of CNTFR with LIFR and gp130. We reported previously that the membrane distal cytokine-binding domain (CBD1) of LIFR could interact in vitro with soluble CNTFR (sCNTFR) in the absence of CNTF. Here we show that the CBD of human gp130 can also bind in vitro to sCNTFR in the absence of CNTF. In addition, the gp130 CBD could compete with the LIFR CBD1 for the binding of sCNTFR. Substitution of residues in the gp130 CBD, the LIFR CBD1, and the CNTFR BC domain that are expected to be involved in receptor-receptor interactions significantly reduced their interactions. An NMR chemical shift perturbation study of the interaction between the BC domains of CNTFR and gp130 further mapped the interaction surface. These data suggest that both the gp130 CBD and the LIFR CBD1 interact with CNTFR in a similar way and provide insights into the nature of the CNTF receptor complex.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.subject.meshAmino Acid Substitutionen_HK
dc.subject.meshAntigens, CD - chemistry - metabolismen_HK
dc.subject.meshBinding Sitesen_HK
dc.subject.meshCytokine Receptor gp130en_HK
dc.subject.meshHumansen_HK
dc.subject.meshLeukemia Inhibitory Factor Receptor alpha Subuniten_HK
dc.subject.meshMembrane Glycoproteins - chemistry - metabolismen_HK
dc.subject.meshModels, Molecularen_HK
dc.subject.meshNuclear Magnetic Resonance, Biomolecularen_HK
dc.subject.meshProtein Bindingen_HK
dc.subject.meshProtein Structure, Tertiaryen_HK
dc.subject.meshReceptor, Ciliary Neurotrophic Factor - chemistry - genetics - metabolismen_HK
dc.subject.meshReceptors, Cytokine - chemistry - metabolismen_HK
dc.subject.meshReceptors, OSM-LIFen_HK
dc.subject.meshSolutionsen_HK
dc.titleSolution structure of the C-terminal domain of the ciliary neurotrophic factor (CNTF) receptor and ligand free associations among components of the CNTF receptor complexen_HK
dc.typeArticleen_HK
dc.identifier.emailSze, KH:khsze@hku.hken_HK
dc.identifier.authoritySze, KH=rp00785en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1074/jbc.M301976200en_HK
dc.identifier.pmid12707266-
dc.identifier.scopuseid_2-s2.0-0038607650en_HK
dc.identifier.hkuros93916en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0038607650&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume278en_HK
dc.identifier.issue26en_HK
dc.identifier.spage23285en_HK
dc.identifier.epage23294en_HK
dc.identifier.isiWOS:000183638600011-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridMan, D=36878997300en_HK
dc.identifier.scopusauthoridHe, W=55218918100en_HK
dc.identifier.scopusauthoridSze, KH=7006735061en_HK
dc.identifier.scopusauthoridGong, K=36900598600en_HK
dc.identifier.scopusauthoridSmith, DK=7410351143en_HK
dc.identifier.scopusauthoridZhu, G=7402633110en_HK
dc.identifier.scopusauthoridIp, NY=7005756760en_HK

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