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dc.contributor.CRUESPUNIVERSIDADE DE ESTADUAL DE CAMPINASpt_BR
dc.identifier.isbn1083-351Xpt
dc.typeArtigo de Periódicopt_BR
dc.titleAn Evaluation Of The Crystal Structure Of C-terminal Truncated Apolipoprotein A-i In Solution Reveals Structural Dynamics Related To Lipid Bindingpt_BR
dc.contributor.authorMelchiorpt_BR
dc.contributor.authorJT; Walkerpt_BR
dc.contributor.authorRG; Morrispt_BR
dc.contributor.authorJ; Jonespt_BR
dc.contributor.authorMK; Segrestpt_BR
dc.contributor.authorJP; Limapt_BR
dc.contributor.authorDB; Carvalhopt_BR
dc.contributor.authorPC; Gozzopt_BR
dc.contributor.authorFC; Castleberrypt_BR
dc.contributor.authorM; Thompsonpt_BR
dc.contributor.authorTB; Davidsonpt_BR
dc.contributor.authorWSpt_BR
unicamp.author.emailTom.Thompson@uc.edu; Sean.Davidson@UC.edupt_BR
dc.subjectApolipoproteinpt_BR
dc.subjectMass Spectrometry (ms)pt_BR
dc.subjectOligomerizationpt_BR
dc.subjectSmall-angle X-ray Scattering (saxs)pt_BR
dc.subjectStructural Biologypt_BR
dc.subjectStructural Modelpt_BR
dc.description.abstractApolipoprotein (apo) A-I mediates many of the anti-atherogenic functions attributed to high density lipoprotein. Unfortunately, efforts toward a high resolution structure of full-length apoA-I have not been fruitful, although there have been successes with deletion mutants. Recently, a C-terminal truncation (apoA-I185-243) was crystallized as a dimer. The structure showed two helical bundles connected by a long, curved pair of swapped helical domains. To compare this structure to that existing under solution conditions, we applied small angle x-ray scattering and isotope-assisted chemical cross-linking to apoA-I185-243 in its dimeric and monomeric forms. For the dimer, we found evidence for the shared domains and aspects of the N-terminal bundles, but not the molecular curvature seen in the crystal. We also found that the N-terminal bundles equilibrate between open and closed states. Interestingly, this movement is one of the transitions proposed during lipid binding. The monomer was consistent with a model in which the long shared helix doubles back onto the helical bundle. Combined with the crystal structure, these data offer an important starting point to understand the molecular details of high density lipoprotein biogenesis.en
dc.relation.ispartofJournal Of Biological Chemistrypt_BR
dc.publisher.cityBETHESDApt_BR
dc.publisherAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INCpt_BR
dc.date.issued2016pt_BR
dc.identifier.citationJournal Of Biological Chemistry. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, n. 291, n. 10, p. 5439 - 5451.pt_BR
dc.language.isoEnglishpt_BR
dc.description.volume291pt_BR
dc.description.issuenumberpt_BR
dc.description.firstpage5439pt_BR
dc.description.lastpage5451pt_BR
dc.rightsfechadopt_BR
dc.sourceWOSpt_BR
dc.identifier.issn1083-351Xpt_BR
dc.identifier.wosidWOS:000371640600051pt_BR
dc.identifier.doi10.1074/jbc.M115.706093pt_BR
dc.identifier.urlhttp://www-jbc-org.ez88.periodicos.capes.gov.br/content/291/10/5439pt_BR
dc.description.sponsorshipNational Institutes of Health [R01 GM098458, HL67093]pt_BR
dc.description.sponsorshipNational Institute of Health Project MINOS [R01GM105404]pt_BR
dc.description.sponsorshipDepartment of Energy Office of Basic Energy Sciences through the Integrated Diffraction Analysis Technologies programpt_BR
dc.description.sponsorshipDepartment of Energy Office of Biological and Environmental Researchpt_BR
dc.date.available2016-12-06T18:31:52Z-
dc.date.accessioned2016-12-06T18:31:52Z-
dc.description.provenanceMade available in DSpace on 2016-12-06T18:31:52Z (GMT). No. of bitstreams: 1 000371640600051.pdf: 3241062 bytes, checksum: 0062da01694c1319d34a1c91dfcfb2fd (MD5) Previous issue date: 2016en
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/320401-
dc.description.conferencelocationpt_BR
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