Cuesta I, Geng X, Asenjo A, Villanueva N
Centro Nacional de Microbiología, Instituto de Salud Carlos III, Majadahonda, Madrid 28220, Spain.
J Virol. 2000 Nov;74(21):9858-67. doi: 10.1128/jvi.74.21.9858-9867.2000.
The structural phosphoprotein M2-1 of human respiratory syncytial virus (HRSV) Long strain shows RNA binding capacity in three different assays that detect RNA-protein complexes: cross-linking, gel retardation, and Northern-Western assays. It is able to bind HRSV leader RNA specifically with cooperative kinetics, with an apparent K(d) of at least 90 nM. It also binds to long RNAs with no sequence specificity. The RNA binding domain has been located between amino acid residues 59 and 85, at the NH(2) terminus of the protein. This region contains the phosphorylatable amino acid residues threonine 56 and serine 58, whose modification decreases the binding capacity of M2-1 protein to long RNAs.
人呼吸道合胞病毒（HRSV）长株的结构磷蛋白M2-1在检测RNA-蛋白质复合物的三种不同试验中显示出RNA结合能力：交联试验、凝胶阻滞试验和Northern-Western试验。它能够以协同动力学特异性结合HRSV前导RNA，表观解离常数（K(d)）至少为90 nM。它也能结合长链RNA，且无序列特异性。RNA结合结构域位于该蛋白NH(2)端的氨基酸残基59至85之间。该区域含有可磷酸化的氨基酸残基苏氨酸56和丝氨酸58，其修饰会降低M2-1蛋白与长链RNA的结合能力。
