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Article: HFIP-induced structures and assemblies of the peptides from the transmembrane domain 4 of membrane protein Nramp1

TitleHFIP-induced structures and assemblies of the peptides from the transmembrane domain 4 of membrane protein Nramp1
Authors
KeywordsAssembly
G169D mutation
Helix
NMR
Nramp1-TM4
Issue Date2006
PublisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www.wiley.com/journals
Citation
Biopolymers - Peptide Science Section, 2006, v. 84 n. 3, p. 329-339 How to Cite?
AbstractMembrane protein Nrampl (natural resistance-associated macrophage protein 1) is a pH-dependent divalent metal cation transporter that regulates macrophage activation in infectious and autoimmune diseases. A naturally occurring glycine to aspartic acid substitution at position 169 (G169D) within the transmembrane domain 4 (TM4) of Nrampl makes mice susceptible to Leishmania donovani, Salmonella typhimurium, and Mycobacterium bovis. Here we present a structural and self-assembling study on two synthetic 24-residue peptides, corresponding to TM4 of mouse Nrampl and its G169D mutant, respectively, in 1,1,1,3,3,3- hexafluoroisopropanol-d 2 (HFIP-d 2) aqueous solution by nuclear magnetic resonance (NMR) spectroscopy. The results show that amphipathic α-helical structures are formed from residue Ile173 to Tyr187 for the wild-type peptide and from Trp168 to Tyr187 for the G169D mutant, respectively. The segment of the N-terminus from Leu167 to Leu172 is poorly structured for the wild-type peptide, whereas it is well defined for the G169D mutant. Both peptides aggregate to form a tetramer and the monomeric peptides in peptide bundles are structurally and orientationally similar. The intermolecular interactions in assemblies could be stronger in the C-terminal regions related to residues Phe180-Leu184 than those in the central helical segments for both peptides. The G169D mutation may change the size of the opening mi the termini of assembly. © 2006 Wiley Periodicals, Inc.
Persistent Identifierhttp://hdl.handle.net/10722/69134
ISSN
2015 Impact Factor: 2.248
2015 SCImago Journal Rankings: 1.199
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorXue, Ren_HK
dc.contributor.authorWang, Sen_HK
dc.contributor.authorWang, Cen_HK
dc.contributor.authorZhu, Ten_HK
dc.contributor.authorLi, Fen_HK
dc.contributor.authorSun, Hen_HK
dc.date.accessioned2010-09-06T06:10:53Z-
dc.date.available2010-09-06T06:10:53Z-
dc.date.issued2006en_HK
dc.identifier.citationBiopolymers - Peptide Science Section, 2006, v. 84 n. 3, p. 329-339en_HK
dc.identifier.issn0006-3525en_HK
dc.identifier.urihttp://hdl.handle.net/10722/69134-
dc.description.abstractMembrane protein Nrampl (natural resistance-associated macrophage protein 1) is a pH-dependent divalent metal cation transporter that regulates macrophage activation in infectious and autoimmune diseases. A naturally occurring glycine to aspartic acid substitution at position 169 (G169D) within the transmembrane domain 4 (TM4) of Nrampl makes mice susceptible to Leishmania donovani, Salmonella typhimurium, and Mycobacterium bovis. Here we present a structural and self-assembling study on two synthetic 24-residue peptides, corresponding to TM4 of mouse Nrampl and its G169D mutant, respectively, in 1,1,1,3,3,3- hexafluoroisopropanol-d 2 (HFIP-d 2) aqueous solution by nuclear magnetic resonance (NMR) spectroscopy. The results show that amphipathic α-helical structures are formed from residue Ile173 to Tyr187 for the wild-type peptide and from Trp168 to Tyr187 for the G169D mutant, respectively. The segment of the N-terminus from Leu167 to Leu172 is poorly structured for the wild-type peptide, whereas it is well defined for the G169D mutant. Both peptides aggregate to form a tetramer and the monomeric peptides in peptide bundles are structurally and orientationally similar. The intermolecular interactions in assemblies could be stronger in the C-terminal regions related to residues Phe180-Leu184 than those in the central helical segments for both peptides. The G169D mutation may change the size of the opening mi the termini of assembly. © 2006 Wiley Periodicals, Inc.en_HK
dc.languageengen_HK
dc.publisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www.wiley.com/journalsen_HK
dc.relation.ispartofBiopolymers - Peptide Science Sectionen_HK
dc.rightsBiopolymers. Copyright © John Wiley & Sons, Inc.en_HK
dc.subjectAssemblyen_HK
dc.subjectG169D mutationen_HK
dc.subjectHelixen_HK
dc.subjectNMRen_HK
dc.subjectNramp1-TM4en_HK
dc.titleHFIP-induced structures and assemblies of the peptides from the transmembrane domain 4 of membrane protein Nramp1en_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0006-3525&volume=84&spage=329&epage=339&date=2006&atitle=HFIP-Induced+Structures+and+Assemblies+of+the+Peptides from+the+Transmembrane+Domain+4+of+Membrane+Protein+Nramp1en_HK
dc.identifier.emailSun, H:hsun@hkucc.hku.hken_HK
dc.identifier.authoritySun, H=rp00777en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1002/bip.20478en_HK
dc.identifier.pmid16479587-
dc.identifier.scopuseid_2-s2.0-33646254607en_HK
dc.identifier.hkuros115871en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33646254607&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume84en_HK
dc.identifier.issue3en_HK
dc.identifier.spage329en_HK
dc.identifier.epage339en_HK
dc.identifier.isiWOS:000236834000009-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridXue, R=35410831500en_HK
dc.identifier.scopusauthoridWang, S=7410349295en_HK
dc.identifier.scopusauthoridWang, C=35235454200en_HK
dc.identifier.scopusauthoridZhu, T=55168295600en_HK
dc.identifier.scopusauthoridLi, F=36079222200en_HK
dc.identifier.scopusauthoridSun, H=7404827446en_HK

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