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Article: Structure, topology and assembly of a 32-mer peptide corresponding to the loop 3 and transmembrane domain 4 of divalent metal transporter (DMT1) in membrane-mimetic environments

TitleStructure, topology and assembly of a 32-mer peptide corresponding to the loop 3 and transmembrane domain 4 of divalent metal transporter (DMT1) in membrane-mimetic environments
Authors
KeywordsDivalent metal transporter (DMT1)
NMR structure
SDS micelles
Transmembrane peptide
Issue Date2008
PublisherElsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/jinorgbio
Citation
Journal Of Inorganic Biochemistry, 2008, v. 102 n. 5-6, p. 1257-1266 How to Cite?
AbstractDivalent metal transporter (DMT1) belongs to the family of Nramp proteins. The fourth transmembrane domain (TM4) housing the disease-causing mutations both in Nramp1 and Nramp2 at the conserved two adjacent glycine residues, was implicated to serve an important biological function. In the present study, we have characterized structurally and topologically a 32-mer synthetic peptide, corresponding to the sequence of the loop 3 and the fourth transmembrane domain of rat DMT1 in membrane-mimetic environments (e.g. TFE, SDS micelles) using both CD and NMR spectroscopic techniques. Solution structures derived from NMR and molecular dynamic/simulated annealing calculation demonstrated that the peptide exhibits a highly defined α-helice in the middle portion of the peptide, flanked by a highly flexible N-terminus and a relatively ordered C-terminus. Paramagnetic broadening on peptide signals by spin-labels and Mn2+ suggested that both the N-terminus and helical core of the peptide were embedded into the SDS micelles. The peptide exhibited amphipathic characteristics, with hydrophilic residues (Thr189, Asp192, Thr193 and Asp200) lying in one side of the helix which provides a basis for the formation of water-filled channel architectures through self-associations. Diffusion-ordered spectroscopy (DOSY) indicated that the peptide exhibits mixtures of hexamers, trimers and monomers, in contrast to the fourth transmembrane peptide (24-mer) being aggregated as a trimer only. This appears to be the first report on the effects of loops on aggregation behavior of transmembrane domains in membrane-mimetic environments. © 2008 Elsevier Inc. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/68861
ISSN
2015 Impact Factor: 3.205
2015 SCImago Journal Rankings: 0.983
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLi, Hen_HK
dc.contributor.authorGu, JDen_HK
dc.contributor.authorSun, Hen_HK
dc.date.accessioned2010-09-06T06:08:23Z-
dc.date.available2010-09-06T06:08:23Z-
dc.date.issued2008en_HK
dc.identifier.citationJournal Of Inorganic Biochemistry, 2008, v. 102 n. 5-6, p. 1257-1266en_HK
dc.identifier.issn0162-0134en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68861-
dc.description.abstractDivalent metal transporter (DMT1) belongs to the family of Nramp proteins. The fourth transmembrane domain (TM4) housing the disease-causing mutations both in Nramp1 and Nramp2 at the conserved two adjacent glycine residues, was implicated to serve an important biological function. In the present study, we have characterized structurally and topologically a 32-mer synthetic peptide, corresponding to the sequence of the loop 3 and the fourth transmembrane domain of rat DMT1 in membrane-mimetic environments (e.g. TFE, SDS micelles) using both CD and NMR spectroscopic techniques. Solution structures derived from NMR and molecular dynamic/simulated annealing calculation demonstrated that the peptide exhibits a highly defined α-helice in the middle portion of the peptide, flanked by a highly flexible N-terminus and a relatively ordered C-terminus. Paramagnetic broadening on peptide signals by spin-labels and Mn2+ suggested that both the N-terminus and helical core of the peptide were embedded into the SDS micelles. The peptide exhibited amphipathic characteristics, with hydrophilic residues (Thr189, Asp192, Thr193 and Asp200) lying in one side of the helix which provides a basis for the formation of water-filled channel architectures through self-associations. Diffusion-ordered spectroscopy (DOSY) indicated that the peptide exhibits mixtures of hexamers, trimers and monomers, in contrast to the fourth transmembrane peptide (24-mer) being aggregated as a trimer only. This appears to be the first report on the effects of loops on aggregation behavior of transmembrane domains in membrane-mimetic environments. © 2008 Elsevier Inc. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherElsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/jinorgbioen_HK
dc.relation.ispartofJournal of Inorganic Biochemistryen_HK
dc.rightsJournal of Inorganic Biochemistry. Copyright © Elsevier Inc.en_HK
dc.subjectDivalent metal transporter (DMT1)en_HK
dc.subjectNMR structureen_HK
dc.subjectSDS micellesen_HK
dc.subjectTransmembrane peptideen_HK
dc.titleStructure, topology and assembly of a 32-mer peptide corresponding to the loop 3 and transmembrane domain 4 of divalent metal transporter (DMT1) in membrane-mimetic environmentsen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0162-0134&volume=102&spage=1257&epage=1266&date=2008&atitle=Structure,+topology+and+assembly+of+a+32-mer+peptide+corresponding+to+the+loop+3+and+transmembrane+domain+4+of+divalent+metal+transporter+(DMT1)+in+membrane-mimetic+environmentsen_HK
dc.identifier.emailGu, JD: jdgu@hkucc.hku.hken_HK
dc.identifier.emailSun, H: hsun@hku.hken_HK
dc.identifier.authorityGu, JD=rp00701en_HK
dc.identifier.authoritySun, H=rp00777en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.jinorgbio.2007.12.019en_HK
dc.identifier.pmid18243325-
dc.identifier.scopuseid_2-s2.0-41949121798en_HK
dc.identifier.hkuros145548en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-41949121798&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume102en_HK
dc.identifier.issue5-6en_HK
dc.identifier.spage1257en_HK
dc.identifier.epage1266en_HK
dc.identifier.isiWOS:000256239600029-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridLi, H=14023043100en_HK
dc.identifier.scopusauthoridGu, JD=7403129601en_HK
dc.identifier.scopusauthoridSun, H=7404827446en_HK

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