The　allosteric　regulation　during　the　binding　interactions　between　small　nuclear　RNAs　(snRNAs)　and　the　associated　protein　factors　is　critical　to　the　function　of　spliceosomes　in　alternative　RNA　splicing.　Although　network　models　combined　with　molecular　dynamics　simulations　have　shown　to　be　powerful　tools　for　the　analysis　of　protein　allostery,　the　atomic-level　simulations　are,　however,　too　expensive　and　with　limited　accuracy　for　the　large-size　systems.　In　this　work,　we　use　a　residual　network　model　combined　with　a　coarse-grained　Gaussian　network　model　(GNM)　to　investigate　the　binding　interactions　between　the　snRNA　and　the　human　U1A　protein　which　is　a　major　component　of　the　spliceosomal　U1　small　nuclear　ribonucleoprotein　particle,　and　to　identify　the　residues　that　play　an　important　role　in　the　allosteric　communication　in　U1A　during　this　process.　We　also　utilize　the　Girvan-Newman　method　to　detect　the　structural　organization　in　U1A-snRNA　recognition　and　interactions.　Our　results　reveal　that:　(I)　not　only　the　residues　at　the　binding　sites　that　are　traditionally　considered　to　play　a　major　role　in　U1A-snRNA　association,　but　those　residues　that　are　far　away　from　the　RNA　binding　interface　participate　in　the　U1A＇s　allosteric　signal　transmission　induced　by　the　RNA　binding;　(H)　the　structure　of　U1A　protein　is　well　organized　with　different　communities　acting　different　roles　for　its　RNA　binding　and　allosteric　regulation.　The　study　demonstrates　that　the　combination　of　the　residual　network　and　elastic　network　models　is　an　effective　and　efficient　method　which　can　be　readily　extended　to　the　investigation　of　the　allosteric　communication　for　other　macromolecular　interaction　systems.