Both Basic and Acidic Amino Acid Residues of Are Involved in Triggering Substate of RyR1英文文献资料.docVIP

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Both Basic and Acidic Amino Acid Residues of Are Involved in Triggering Substate of RyR1英文文献资料.doc

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Both Basic and Acidic Amino Acid Residues of Are Involved in Triggering Substate of RyR1英文文献资料

HindawiPublishingCorporation JournalofBiomedicineandBiotechnology Volume2011,ArticleID386384,10pages doi:10.1155/2011/386384 ResearchArticle BothBasicandAcidicAminoAcidResiduesofIpTxaAreInvolved inTriggeringSubstateofRyR1 InRaSeo,1,2DaeEunKang,1,2DongWooSong,1,2andDoHanKim 1,2 1 2 SystemsBiologyResearchCenter,GwangjuInstituteofScienceandTechnology(GIST),Gwangju500-712,RepublicofKorea SchoolofLifeSciences,GwangjuInstituteofScienceandTechnology(GIST),1Oryong-dong,Buk-gu, Gwangju500-712,RepublicofKorea CorrespondenceshouldbeaddressedtoDoHanKim,dhkim@gist.ac.kr Received1June2011;Revised5August2011;Accepted10August2011 AcademicEditor:AikateriniKontrogianni-Konstantopoulos Copyright?2011InRaSeoetal.ThisisanopenaccessarticledistributedundertheCreativeCommonsAttributionLicense, whichpermitsunrestricteduse,distribution,andreproductioninanymedium,providedtheoriginalworkisproperlycited. ImperatoxinA(IpTxa)isknowntomodifythegatingofskeletalryanodinereceptor(RyR1).Inthispaper,theabilityofcharged aaresiduesofIpTxatoinducesubstateofnativeRyR1inHSRwasexamined.Ourresultsshowthatthebasicresidues(e.g.,Lys 19 , , Lys 20 ,Lys andArg substate.ResiduessuchasLys 22 ,Arg )neartheC-terminusandsomeacidicresidues(e.g.,Glu andThr maybeinvolvedintheself-regulationofsubstateofRyR1,sincealaninesubstitutionof 23 ,andArg 24 )areimportantforproducingsubstateofRyR1.Inaddition,otherbasicresidues(e.g.,Lys 30 ,Arg 31 33 29 ,Asp ,andAsp 13 2 )arealsoinvolvedinthegenerationof 8 26 theaaresiduesledtoadrasticconversiontothesubstate.Themodi?cationsofthechannelgatingbythewild-typeandmutant toxinsweresimilarinpuri?edRyR1.Takentogether,thespeci?cchargedistributionsonthesurfaceofIpTxa areessentialfor regulationofthechannelgatingofRyR1. 1.Introduction fragmentofII-IIIloopregionofskeletalDHPR(PeptideA) alsobindtoRyR1andmodifychannelactivity[15–18].MCa alsostronglyenhances[3H]ryanodinebindingtoRyR1and Instriatedmuscles,depolarizationofthecellsurfacemem- branesleadstoactivationofryanodinereceptor