Mitochondrial Pyruvate Carrier 1 and 2 Heterodimer, In Silico, Models of Plant and Human Complexes: A Comparison of Structure and Transporter Binding Properties
{"title":"Mitochondrial Pyruvate Carrier 1 and 2 Heterodimer, In Silico, Models of Plant and Human Complexes: A Comparison of Structure and Transporter Binding Properties","authors":"Jason L. Dugan, Allen K. Bourdon, C. Phelix","doi":"10.4018/IJKDB.2017070102","DOIUrl":null,"url":null,"abstract":"Theplantandhumanmitochondrialpyruvatecarrier(MPC)hadbeenstudiedinthe1970s-1990s providingmanypredictionsonfunctionalproteinstructureandmechanismsofsubstratebinding.Genes forhumanandplantMPChavebeenidentified,butnocrystalstructurehasyetbeenregisteredor depositedinaproteindatabank.Thisreportdescribesresultsforcomparisonsofstructureforhuman andplantMPC1/2heterodimerhomologymodels.Keycysteineresiduesareidentifiedforpyruvate andblockerbindingandformationofthiohemiacetalorMichaeladditionbonds.Evidenceisprovided foranalternatingaccessmodelinhuman,mouseear-cress,castorandcommonbeans,andcorn. KeywoRDS Arabidopsis Thaliana, Homo Sapien, In Silico, Phaseolus Vulgaris, Protein Homology, Protein Protein Docking, Pyruvate Docking, Ricinus Communis, Zea Mays","PeriodicalId":160270,"journal":{"name":"Int. J. Knowl. Discov. Bioinform.","volume":"14 1","pages":"0"},"PeriodicalIF":0.0000,"publicationDate":"2017-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"5","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Int. J. Knowl. Discov. Bioinform.","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.4018/IJKDB.2017070102","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 5
Abstract
Theplantandhumanmitochondrialpyruvatecarrier(MPC)hadbeenstudiedinthe1970s-1990s providingmanypredictionsonfunctionalproteinstructureandmechanismsofsubstratebinding.Genes forhumanandplantMPChavebeenidentified,butnocrystalstructurehasyetbeenregisteredor depositedinaproteindatabank.Thisreportdescribesresultsforcomparisonsofstructureforhuman andplantMPC1/2heterodimerhomologymodels.Keycysteineresiduesareidentifiedforpyruvate andblockerbindingandformationofthiohemiacetalorMichaeladditionbonds.Evidenceisprovided foranalternatingaccessmodelinhuman,mouseear-cress,castorandcommonbeans,andcorn. KeywoRDS Arabidopsis Thaliana, Homo Sapien, In Silico, Phaseolus Vulgaris, Protein Homology, Protein Protein Docking, Pyruvate Docking, Ricinus Communis, Zea Mays