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Oligomeric Interfaces Under the Lens Gemini 英文参考文献
OligomericInterfacesUndertheLens:Gemini
GiovanniFeverati,ClaireLesieur*
Laboratoiredephysiquethe′oriqueLAPTH,CNRS,UMR5108associe′ a` l’Universite′ deSavoie,BP110,AnnecyleVieux,France
Abstract
Theassemblyofsubunitsinproteinoligomersisanimportanttopictostudyasavastnumberofproteinsexistsasstableor
transientoligomerandbecauseitisamechanismusedbysomeproteinoligomersforkillingcells(e.g.,perforinfromthe
humanimmunesystem,pore-formingtoxinsfrombacteria,phage,amoeba,proteinmisfoldingdiseases,etc.).Onlyafewof
the amino acids that constitute a protein oligomer seem to regulate the capacity of the protein to assemble (to form
interfaces),andsomeoftheseaminoacidsarelocalizedattheinterfacesthatlinkthedifferentchains.Theidentificationof
theresiduesoftheseinterfacesisratherdifficult.Wehavedevelopedaseriesofprograms,underthecommonnameof
Gemini,thatcanselectthesubsetoftheresiduesthatisinvolvedintheinterfacesofaproteinoligomerofknownatomic
structure, and generate a 2D interaction network (or graph) of the subset. The graphs generated for several oligomers
demonstratetheaccuracyoftheselectionofsubsetsthatareinvolvedinthegeometricalandthechemicalpropertiesof
interfaces.TheresultsoftheGeminiprogramsareingoodagreementwiththoseofsimilarprogramswithanadvantage
thatGeminiprogramscanperformtheresidueselectionmuchmorerapidly.Moreover,Geminiprogramscanalsoperform
onasingleproteinoligomerwithouttheneedofcomparisonpartners.Thegraphsareextremelyusefulforcomparative
studiesthatwouldhelpinaddressingquestionsnotonlyonthesequencespecificityofproteininterfacesbutalsoonthe
mechanismoftheassemblyofunrelatedproteinoligomers.
Citation:FeveratiG,LesieurC(2010)OligomericInterfacesUndertheLens:Gemini.PLoSONE5(3):e9897.doi:10.1371/journal.pone.0009897
Editor:MarkusJ.Buehler,MassachusettsInstituteofTechnology,UnitedStatesofAmerica
ReceivedAugust11,2009;AcceptedMarch2,2010;PublishedMarch25,2010
Copyright: ?2010 Feverati, Lesieur. Thisisanopen-access article distributedunder theterms oftheCreativeCommons
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