File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Structural prediction of the β-domain of metallothionein-3 by molecular dynamics simulation

TitleStructural prediction of the β-domain of metallothionein-3 by molecular dynamics simulation
Authors
Issue Date2007
Citation
Proteins: Structure, Function And Genetics, 2007, v. 68 n. 1, p. 255-266 How to Cite?
AbstractThe β-domain of metallothionein-3 (MT3) has been reported to be crucial to the neuron growth inhibitory bioactivity. Little detailed three-dimensional structural information is available to present a reliable basis for elucidation on structure-property-function relationships of this unique protein by experimental techniques. So, molecular dynamics simulation is adopted to study the structure of β-domain of MT3. In this article, a 3D structural model of β-domain of MT3 was generated. The molecular simulations provide detailed protein structural information of MT3. As compared with MT2, we found a characteristic conformation formed in the fragment (residue 1-13) at the N-terminus of MT3 owing to the constraint induced by 5TCPCP 9, in which Pro7 and Pro9 residues are on the same side of the protein, both facing outward and the two 5-member rings of prolines are arranged almost in parallel, while Thr5 is on the opposite side. Thr5 in MT3 is also found to make the first four residues relatively far from the fragment (residue 23-26) as compared with MT2. The simulated structure of β-domain of MT3 is looser than that of MT2. The higher energy of MT3 than that of MT2 calculated supports these conclusions. Simulation on the four isomer arising from the cis- or trans-configuration of 6CPCP 9 show that the trans-/trans-isomer is energetic favorable. The partially unfolding structure of β-domain of MT3 is also simulated and the results show the influence of 6CPCP 9 sequence on the correct folding of this domain. The correlations between the bioactivity of MT3 and the simulated structure as well as the folding of β-domain of MT3 are discussed based on our simulation and previous results. © 2007 Wiley-Liss, Inc.
Persistent Identifierhttp://hdl.handle.net/10722/168117
ISSN
2015 Impact Factor: 2.499
2015 SCImago Journal Rankings: 1.383
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorNi, FYen_US
dc.contributor.authorCai, Ben_US
dc.contributor.authorDing, ZCen_US
dc.contributor.authorZheng, Fen_US
dc.contributor.authorZhang, MJen_US
dc.contributor.authorWu, HMen_US
dc.contributor.authorSun, HZen_US
dc.contributor.authorHuang, ZXen_US
dc.date.accessioned2012-10-08T03:15:17Z-
dc.date.available2012-10-08T03:15:17Z-
dc.date.issued2007en_US
dc.identifier.citationProteins: Structure, Function And Genetics, 2007, v. 68 n. 1, p. 255-266en_US
dc.identifier.issn0887-3585en_US
dc.identifier.urihttp://hdl.handle.net/10722/168117-
dc.description.abstractThe β-domain of metallothionein-3 (MT3) has been reported to be crucial to the neuron growth inhibitory bioactivity. Little detailed three-dimensional structural information is available to present a reliable basis for elucidation on structure-property-function relationships of this unique protein by experimental techniques. So, molecular dynamics simulation is adopted to study the structure of β-domain of MT3. In this article, a 3D structural model of β-domain of MT3 was generated. The molecular simulations provide detailed protein structural information of MT3. As compared with MT2, we found a characteristic conformation formed in the fragment (residue 1-13) at the N-terminus of MT3 owing to the constraint induced by 5TCPCP 9, in which Pro7 and Pro9 residues are on the same side of the protein, both facing outward and the two 5-member rings of prolines are arranged almost in parallel, while Thr5 is on the opposite side. Thr5 in MT3 is also found to make the first four residues relatively far from the fragment (residue 23-26) as compared with MT2. The simulated structure of β-domain of MT3 is looser than that of MT2. The higher energy of MT3 than that of MT2 calculated supports these conclusions. Simulation on the four isomer arising from the cis- or trans-configuration of 6CPCP 9 show that the trans-/trans-isomer is energetic favorable. The partially unfolding structure of β-domain of MT3 is also simulated and the results show the influence of 6CPCP 9 sequence on the correct folding of this domain. The correlations between the bioactivity of MT3 and the simulated structure as well as the folding of β-domain of MT3 are discussed based on our simulation and previous results. © 2007 Wiley-Liss, Inc.en_US
dc.languageengen_US
dc.relation.ispartofProteins: Structure, Function and Geneticsen_US
dc.subject.meshAmino Acid Motifs - Geneticsen_US
dc.subject.meshAnimalsen_US
dc.subject.meshBiophysical Phenomenaen_US
dc.subject.meshBiophysicsen_US
dc.subject.meshCadmium - Chemistryen_US
dc.subject.meshComputer Simulationen_US
dc.subject.meshModels, Molecularen_US
dc.subject.meshNerve Tissue Proteins - Chemistryen_US
dc.subject.meshProtein Structure, Secondaryen_US
dc.subject.meshProtein Structure, Tertiaryen_US
dc.subject.meshSulfur - Chemistryen_US
dc.titleStructural prediction of the β-domain of metallothionein-3 by molecular dynamics simulationen_US
dc.typeArticleen_US
dc.identifier.emailSun, HZ:hsun@hkucc.hku.hken_US
dc.identifier.authoritySun, HZ=rp00777en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1002/prot.21404en_US
dc.identifier.pmid17427961-
dc.identifier.scopuseid_2-s2.0-34249912942en_US
dc.identifier.hkuros132933-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-34249912942&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume68en_US
dc.identifier.issue1en_US
dc.identifier.spage255en_US
dc.identifier.epage266en_US
dc.identifier.isiWOS:000246894800026-
dc.identifier.scopusauthoridNi, FY=9841840800en_US
dc.identifier.scopusauthoridCai, B=36484162900en_US
dc.identifier.scopusauthoridDing, ZC=14424225400en_US
dc.identifier.scopusauthoridZheng, F=55188977900en_US
dc.identifier.scopusauthoridZhang, MJ=7601555100en_US
dc.identifier.scopusauthoridWu, HM=13808047800en_US
dc.identifier.scopusauthoridSun, HZ=7404827446en_US
dc.identifier.scopusauthoridHuang, ZX=7406221847en_US

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats