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Article: Solution structure and dynamics of human metallothionein-3 (MT-3)

TitleSolution structure and dynamics of human metallothionein-3 (MT-3)
Authors
KeywordsDynamics
Growth inhibitory factor
Metallothionein-3
NMR
Structures
Zinc
Issue Date2006
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febslet
Citation
Febs Letters, 2006, v. 580 n. 3, p. 795-800 How to Cite?
AbstractAlzheimer's disease is characterized by progressive loss of neurons accompanied by the formation of intraneural neurofibrillary tangles and extracellular amyloid plaques. Human neuronal growth inhibitory factor, classified as metallothionein-3 (MT-3), was found to be related to the neurotrophic activity promoting cortical neuron survival and dendrite outgrowth in the cell culture studies. We have determined the solution structure of the α-domain of human MT-3 (residues 32-68) by multinuclear and multidimensional NMR spectroscopy in combination with the molecular dynamic simulated annealing approach. The human MT-3 shows two metal-thiolate clusters, one in the N-terminus (β-domain) and one in the C-terminus (α-domain). The overall fold of the α-domain is similar to that of mouse MT-3. However, human MT-3 has a longer loop in the acidic hexapeptide insertion than that of mouse MT-3. Surprisingly, the backbone dynamics of the protein revealed that the β-domain exhibits similar internal motion to the α-domain, although the N-terminal residues are more flexible. Our results may provide useful information for understanding the structure-function relationship of human MT-3. © 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/69943
ISSN
2015 Impact Factor: 3.519
2015 SCImago Journal Rankings: 2.026
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWang, Hen_HK
dc.contributor.authorZhang, Qen_HK
dc.contributor.authorCai, Ben_HK
dc.contributor.authorLi, Hen_HK
dc.contributor.authorSze, KHen_HK
dc.contributor.authorHuang, ZXen_HK
dc.contributor.authorWu, HMen_HK
dc.contributor.authorSun, Hen_HK
dc.date.accessioned2010-09-06T06:18:16Z-
dc.date.available2010-09-06T06:18:16Z-
dc.date.issued2006en_HK
dc.identifier.citationFebs Letters, 2006, v. 580 n. 3, p. 795-800en_HK
dc.identifier.issn0014-5793en_HK
dc.identifier.urihttp://hdl.handle.net/10722/69943-
dc.description.abstractAlzheimer's disease is characterized by progressive loss of neurons accompanied by the formation of intraneural neurofibrillary tangles and extracellular amyloid plaques. Human neuronal growth inhibitory factor, classified as metallothionein-3 (MT-3), was found to be related to the neurotrophic activity promoting cortical neuron survival and dendrite outgrowth in the cell culture studies. We have determined the solution structure of the α-domain of human MT-3 (residues 32-68) by multinuclear and multidimensional NMR spectroscopy in combination with the molecular dynamic simulated annealing approach. The human MT-3 shows two metal-thiolate clusters, one in the N-terminus (β-domain) and one in the C-terminus (α-domain). The overall fold of the α-domain is similar to that of mouse MT-3. However, human MT-3 has a longer loop in the acidic hexapeptide insertion than that of mouse MT-3. Surprisingly, the backbone dynamics of the protein revealed that the β-domain exhibits similar internal motion to the α-domain, although the N-terminal residues are more flexible. Our results may provide useful information for understanding the structure-function relationship of human MT-3. © 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febsleten_HK
dc.relation.ispartofFEBS Lettersen_HK
dc.rightsF E B S Letters. Copyright © Elsevier BV.en_HK
dc.subjectDynamicsen_HK
dc.subjectGrowth inhibitory factoren_HK
dc.subjectMetallothionein-3en_HK
dc.subjectNMRen_HK
dc.subjectStructuresen_HK
dc.subjectZincen_HK
dc.subject.meshAlzheimer Disease - metabolismen_HK
dc.subject.meshAmyloid - chemistry - metabolismen_HK
dc.subject.meshAnimalsen_HK
dc.subject.meshCell Survivalen_HK
dc.subject.meshDendrites - metabolismen_HK
dc.subject.meshHumansen_HK
dc.subject.meshMiceen_HK
dc.subject.meshNerve Tissue Proteins - chemistry - metabolismen_HK
dc.subject.meshNuclear Magnetic Resonance, Biomolecularen_HK
dc.subject.meshProtein Structure, Secondaryen_HK
dc.subject.meshProtein Structure, Tertiaryen_HK
dc.subject.meshStructure-Activity Relationshipen_HK
dc.titleSolution structure and dynamics of human metallothionein-3 (MT-3)en_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0014-5793&volume=580&spage=795&epage=800&date=2006&atitle=Solution+structure+and+dynamics+of+human+metallothionein-3+(MT-3)en_HK
dc.identifier.emailSze, KH:khsze@hku.hken_HK
dc.identifier.emailSun, H:hsun@hkucc.hku.hken_HK
dc.identifier.authoritySze, KH=rp00785en_HK
dc.identifier.authoritySun, H=rp00777en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.febslet.2005.12.099en_HK
dc.identifier.pmid16413543-
dc.identifier.scopuseid_2-s2.0-31444449685en_HK
dc.identifier.hkuros114085en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-31444449685&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume580en_HK
dc.identifier.issue3en_HK
dc.identifier.spage795en_HK
dc.identifier.epage800en_HK
dc.identifier.isiWOS:000235222500014-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridWang, H=15052706700en_HK
dc.identifier.scopusauthoridZhang, Q=35515964300en_HK
dc.identifier.scopusauthoridCai, B=36484162900en_HK
dc.identifier.scopusauthoridLi, H=14023043100en_HK
dc.identifier.scopusauthoridSze, KH=7006735061en_HK
dc.identifier.scopusauthoridHuang, ZX=7406221847en_HK
dc.identifier.scopusauthoridWu, HM=7405580635en_HK
dc.identifier.scopusauthoridSun, H=7404827446en_HK
dc.identifier.citeulike3813377-

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