BIOPHYSICAL STUDIES OF RETROVIRAL NUCLEIC ACID INTERACTIVE PROTEINS: HIV

来自HIV-1的核衣壳（NC）蛋白p7是HIV-1的免疫调节所必需的。 基因组RNA的包装。 蛋白质（55个残基）含有两个锌 指和一个单一的色氨酸残基参与核酸 通过与核碱基的堆积相互作用结合。 我们有 表征了金属的寿命和动态各向异性特性， 游离和结合各种二价离子（Zn 2+，Cd 2+，Co 2+）， 与DNA和RNA寡核苷酸的复合物。 Trp的扰动 正在研究寡核苷酸结合后的荧光团， 提供了一个模型的相互作用，嵌入芳香残基 with nucleic核酸lattices晶格. 一系列截短和点突变的 序列已被用来表明，有一个短暂的相互作用 其中两个锌指非常接近。 这些研究 正在扩展其他HIV-1蛋白（逆转录 整合酶）以及分离自不同 逆转录病毒（SIV，HTLV-1）

The nucleocapsid (NC) protein p7 from HIV-1 is required for packaging of genomic RNA. The protein (55 residues) contains two zinc fingers and a single Trp residue that is involved in nucleic acid binding through stacking interactions with nucleobases. We have characterized the lifetime and dynamic anisotropy properties of metal free and bound to various divalent ions (Zn2+, Cd2+, Co2+) and in complexes with DNA and RNA oligonucleotides. Perturbations of the Trp fluorophore upon oligonucleotide binding are being investigated to provide a model for the interaction of intercalating aromatic residues with nucleic acid lattices. A series of truncated and point mutated sequences have been used to show that there is a transient interaction in which the two zinc fingers are in close proximity. These studies are being extended other HIV-1 proteins (reverse transcription integrase) as well as to nucleocapsid proteins isolated from different retroviruses (SIV, HTLV-1)