英语翻译
CDR-H3residesinthecenteroftheP5a/P5chelicalinterfaceat
thethree-helixjunction(Fig.5A).ResiduesGly-98,Ser-100,and
Thr100ainteractwiththewideandshallowminorgrooveofP5cvia
directHbonds,andTyr-102contactsP5abyHbondingtoU131in
theminorgroove.SeveralCDR-H3residuesformapocket(Fig.
5B)thatenclosesU130,thebulgeduridineinP5a,andtheyusea
varietyofmolecularstrategiestointeractwithU130.Arg-94,
Ala-96,Asp-101,andGly100cformdirectHbondstotheuracil
baseandsugarring,whereasthesidechainsofAla-96andMet-99
embracethenucleotidewithnonpolarcontacts.Tyr100bstacks
perpendicularlywiththebase,andArg-94formsanN-Obridgetype
ofionpairwiththeadjacentphosphate(36).Interestingly,
althoughArg-95wasselectedfromthelibrary,itmakesnointeraction
withtheRNAinthestructure;instead,itssidechainpoints
awayfromtheRNAandmakeshydrogenbondinginteractionswith
thebackbonecarbonylgroupsofTyr100bandMet-99,possibly
stabilizingtheCDR-H3loopconformation.
CDR-L2loopresidues(definedasresidues50–56)(37)andthe
flankingframeworkresiduesinteractextensivelywithRNA,mainly
intheP5aminorgroove.ResiduesSer-56,Gly-57,andSer-60form
directHbondstothe32strandofP5a,acrossfromU130nearthe
hingeregion(Fig.5A).Apossiblelong-rangeionpairbetween
Arg-61andthephosphatemoietyofC197maystabilizethis
interaction.DirectHbondingbetweenSer-50andtheU167
phosphatelinksCDR-L2toP5c,makingL2anotherCDRthat
bindsbothhelicalstems.Tyr-49andTyr-55stackperpendicularly
withU130fromthenonpolarsidetosealtheU130-bindingpocket
generatedbyCDR-H3(Fig.5B).Threewatermoleculesorganized
bythefourtyrosineresiduessurroundingU130interactwiththe
sugar–phosphatemoiety,whichmayfurtherstrengthentheRNAFab
interactionatthenonpolarinterfaceoftheU130binding
pocket(Fig.5C).
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