Structural libraries of protein models for multiple species to understand evolution of the renin-angiotensin system

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dc.contributor.authorProkop, Jeremy W.
dc.contributor.authorPetri, Victoria
dc.contributor.authorShimoyama, Mary E.
dc.contributor.authorWatanabe, Ingrid K. M. [UNIFESP]
dc.contributor.authorCasarini, Dulce E. [UNIFESP]
dc.contributor.authorLeeper, Thomas C.
dc.contributor.authorBilinovich, Stephanie M.
dc.contributor.authorJacob, Howard J.
dc.contributor.authorSantos, Robson A. S.
dc.contributor.authorMartins, Almir S.
dc.contributor.authorAraujo, Fabiano C.
dc.contributor.authorReis, Fernando M.
dc.contributor.authorMilsted, Amy
dc.contributor.institutionMed Coll Wisconsin
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionUniv Akron
dc.contributor.institutionUniversidade Federal de Minas Gerais (UFMG)
dc.date.accessioned2016-01-24T14:40:28Z
dc.date.available2016-01-24T14:40:28Z
dc.date.issued2015-05-01
dc.description.abstractThe details of protein pathways at a structural level provides a bridge between genetics/molecular biology and physiology. the renin-angiotensin system is involved in many physiological pathways with informative structural details in multiple components. Few studies have been performed assessing structural knowledge across the system. This assessment allows use of bioinformatics tools to fill in missing structural voids. in this paper we detail known structures of the renin-angiotensin system and use computational approaches to estimate and model components that do not have their protein structures defined. With the subsequent large library of protein structures, we then created a species specific protein library for human, mouse, rat, bovine, zebrafish, and chicken for the system. the rat structural system allowed for rapid screening of genetic variants from 51 commonly used rat strains, identifying amino acid variants in angiotensinogen, ACE2, and AT1b that are in contact positions with other macromolecules. We believe the structural map will be of value for other researchers to understand their experimental data in the context of an environment for multiple proteins, providing pdb files of proteins for the renin-angiotensin system in six species. With detailed structural descriptions of each protein, it is easier to assess a species for use in translating human diseases with animal models. Additionally, as whole genome sequencing continues to decrease in cost, tools such as molecular modeling will gain use as an initial step in designing efficient hypothesis driven research, addressing potential functional outcomes of genetic variants with precompiled protein libraries aiding in rapid characterizations. (C) 2014 Elsevier Inc. All rights reserved.en
dc.description.affiliationMed Coll Wisconsin, Human Mol & Genet Ctr, Milwaukee, WI 53226 USA
dc.description.affiliationMed Coll Wisconsin, Dept Physiol, Milwaukee, WI 53226 USA
dc.description.affiliationMed Coll Wisconsin, Dept Surg, Milwaukee, WI 53226 USA
dc.description.affiliationUniversidade Federal de São Paulo, Dept Med, Div Nephrol, São Paulo, SP, Brazil
dc.description.affiliationUniv Akron, Dept Chem, Akron, OH 44325 USA
dc.description.affiliationMed Coll Wisconsin, Dept Pediat, Milwaukee, WI 53226 USA
dc.description.affiliationUniv Fed Minas Gerais, Inst Ciencias Biol, Dept Fisiol & Biofis, Belo Horizonte, MG, Brazil
dc.description.affiliationUniv Fed Minas Gerais, Dept Obstet & Gynecol, Sch Med, Natl Inst Sci & Technol Mol Med, Belo Horizonte, MG, Brazil
dc.description.affiliationUniv Akron, Dept Biol, Akron, OH 44325 USA
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Med, Div Nephrol, São Paulo, SP, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipAmerican Heart Association
dc.description.sponsorshipOhio Board of Regents Choose Ohio First Bioinformatics initiative award
dc.description.sponsorshipUniversity of Akron, NIH
dc.description.sponsorshipBrazilian National Institute of Science and Technology in Hormones and Women's Health
dc.description.sponsorshipFederal University of Minas Gerais
dc.description.sponsorshipIDAmerican Heart Association: 11PRE7380033
dc.description.sponsorshipIDUniversity of Akron, NIH: 5R01HL064541-15
dc.format.extent106-116
dc.identifierhttp://dx.doi.org/10.1016/j.ygcen.2014.09.010
dc.identifier.citationGeneral and Comparative Endocrinology. San Diego: Academic Press Inc Elsevier Science, v. 215, p. 106-116, 2015.
dc.identifier.doi10.1016/j.ygcen.2014.09.010
dc.identifier.issn0016-6480
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/39057
dc.identifier.wosWOS:000354910900010
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofGeneral and Comparative Endocrinology
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectSequence-to-structure-to-function analysisen
dc.subjectRat geneticsen
dc.subjectComparative modelingen
dc.subjectRenin-angiotensin systemen
dc.subjectAngiotensin peptidesen
dc.titleStructural libraries of protein models for multiple species to understand evolution of the renin-angiotensin systemen
dc.typeinfo:eu-repo/semantics/article
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