UNDERSTANDING PROTEIN-NUCLEIC ACID INTERACTIONS

CC-HH手指的结构和相互作用机制是什么 与核酸的结构域？ 这个问题是通过详细的 几种已知核酸指状区的结构分析 结合蛋白 一个锌指蛋白的数据库已经建立 为了对个体进行统计和结构建模， 手指区域。 建立锌指数据库， 完整的潜在锌指基因序列， 研究界的成员迅速搜索，以防止 测序工作的重大重复。 此集合包含两个 已发表和未发表的基因序列数据。 数据库可用 用于在DCRT Convex 240上进行序列比较。 服务到 研究界提供的是，新的锌指基因序列是e- 邮寄到NIH，添加到数据库，并对结果进行FASTA搜索， 返回时没有对齐。 统计数据的直方图 搜索结果的分布和潜在分数的列表是 包括. 当与未发布的序列匹配时， 并返回提交作者的联系信息， 有关各方可以相互通信。 收集日期 包含147个不同的条目。 这一系列功能性的 相关序列为多序列提供了极好的问题集 比对和基序分析测试。 这些数据的统计分析揭示了5个重复类的CC-HH 锌指结构域的长度范围为27至32个氨基酸， 不同的重复模式。 此外， 最大的一类结构域，29个氨基酸重复长度，揭示了一个显着的 当存在精氨酸或谷氨酰胺时，丝氨酸或苏氨酸的保守 在指状结构域的DNA结合区中。 之间的相关性 建立了核酸序列并观察到了一些结构域。 约束分子动力学模拟表明，有两个 锌指结构域的一般折叠基序。 含序列的域 与共有结构一致的可以采用折叠类似于 公开了ZF 268蛋白质/DNA共晶体的X射线数据。 虽然非- 共有结构采用灵活的β环构象，同源性- 基于分子模型，使用已发表的X射线晶体学数据， 在建 这些基于同源性的结构模型将被用于 用于分子对接实验，以探索DNA序列的能量学 识别.

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 This collection contains both published and unpublished gene sequence data.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 When a match to an unpublished sequence occurs, then the name and contact information of the submitting author is returned so the concerned parties may correspond with each other.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.