UNDERSTANDING PROTEIN-NUCLEIC ACID INTERACTIONS

CC-HH指相互作用的结构和机制是什么 含有核酸的区域？这个问题是通过一个详细的 几种已知核酸指状区的结构分析 结合蛋白。一个锌指蛋白数据库已经建立 为了对个人进行统计和结构建模 手指区域。建立了锌手指数据库，以积累 完整收集潜在的锌指基因序列，可能 被研究界成员迅速搜索，以防止 测序工作的主要重复。此集合既包含 已公布和未公布的基因序列数据。数据库可用 用于DCRT Convex 240上的序列比较。将服务提供给 提供的研究社区是新的锌指基因序列是e- 邮寄给NIH，添加到数据库中，对结果进行快速搜索是 在没有路线的情况下返回。统计量的直方图 搜索结果的分布和潜在得分的列表如下 包括在内。当出现与未发布序列的匹配时，则名称 并返回提交作者的联系信息，因此 有关各方可以相互通信。为收藏注明日期 包含147个不同的条目。这一功能上的大型集合 相关序列为多序列提供了极好的问题集 比对和主题分析测试。 对这些数据的统计分析揭示了CC-HH的5个重复类别 锌指结构域的长度从27到32个氨基酸和22个氨基酸不等 不同的重复模式。此外，还包括 最大的一类结构域，29个氨基酸重复长度，揭示了一个值得注意的 当有精氨酸或谷氨酰胺时丝氨酸或苏氨酸的保守性 在指状域的DNA结合区。两者之间的相关性 建立了核酸序列，并观察到了一些结构域。 受约束的分子动力学模拟表明有两个 锌指结构域的一般折叠图案。具有序列的结构域 一致的共识结构可以采用类似于折叠的 公布了zf268蛋白质/DNA共晶体的X射线数据。而非- 共识结构采用灵活的β环构象，同源- 基于公布的x射线结晶学数据的分子模型是 正在建设中。这些基于同源的结构模型将被使用 用于分子对接实验以探索DNA序列的能量学 承认。

What is the structure and mechanism of interaction of the CC-HH finger domains with nucleic acids? This question is addressed through a detailed structural analysis of the finger regions from several known nucleic acid binding proteins. A database of Zinc Finger proteins has been assembled for the purpose of statistical and structural modeling of the individual finger regions. The Zinc Finger Database was established to accumulate a complete collection of potential zinc finger gene sequences that could be rapidly searched by the members of the research community to prevent a major duplication of sequencing efforts. This collection contains both published and unpublished gene sequence data. The database is available for sequence comparisons on the DCRT Convex 240. The service to the research community provided is that new zinc finger gene sequences are e- mailed to the NIH, added to database, and a FASTA search of the results is returned without the alignments. A histogram of the statistical distribution of the search results and listing of the potential scores is included. When a match to an unpublished sequence occurs, then the name and contact information of the submitting author is returned so the concerned parties may correspond with each other. To date the collection contains 147 different entries. This large collection of functionally related sequences has provided excellent problem set for multiple sequence alignment and motif analysis tests. Statistical analysis of these data has revealed 5 repeat classes of CC-HH zinc finger domains ranging in length from 27 to 32 amino acids and 22 different repeat patterns. Furthermore, compositional statistics of the largest class of domains, 29 amino acid repeat length, reveals a remarkable conservation of serine or threonine when there is an arginine or glutamine in the DNA binding region of the finger domain. A correlation between the nucleic acid sequence was established and some domains have been observed. Constrained molecular dynamics simulations suggest that there are two general folding motifs for the zinc finger domains. Domains with sequences consistent with the consensus structure can adopt fold similar to the published x-ray data for the zf268 protein/dna co-crystal. While non- consensus structures adopt a flexible beta loop conformation, homology- based molecular models using the published x-ray crystallographic data are under construction. These homology-based structural models will be used for molecular docking experiments to explore the energetics of DNA sequence recognition.