Detail Binding of the Human Prp31 Nop Domain to a Composite RNA-Protein Platform in U4 snRNP   Oleh:  Liu, Sunbin ; Dybkov, Olexandr ; Nottrott, Stephanie ; Hartmuth, Klaus ; Liihrmann, Reinhard ; Carlomagno, Teresa ; Wahl, Markus C. Jenis: Article from Bulletin/Magazine Dalam koleksi: SCIENCE (keterangan: ada di Proquest) vol. 316 no. 5821 (Apr. 2007), page 115. Ketersediaan Perpustakaan FK Nomor Panggil: S01.K.2007.04 Non-tandon: 1 (dapat dipinjam: 0) Tandon: tidak ada     Lihat Detail Induk Isi artikel recognize different ribonucleoprotein (RNP) particles. hPrp31 interacts with complexes containing the lS.SK protein and U4 or U4atac small nuclear RNA (snRNA), whereas NopS6/S8 associate with lS.SK-box CID small nucleolar RNA complexes. We present structural and biochemical analyses of hPrp31-1S.SK-U4 snRNA complexes that show how the conserved Nop domain in hPrp31 maintains high RNP binding selectivity despite relaxed RNA sequence requirements. The Nop domain is a genuine RNP binding module, exhibiting RNA and protein binding surfaces. Yeast two-hybrid analyses suggest a link between retinitis pigmentosa and an aberrant hPrp31-hPrp6 interaction that blocks U4/U6-US tri-snRNP formation. Opini Anda Klik untuk menuliskan opini Anda tentang koleksi ini! Kembali

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