ANALYSIS OF PACKING CONTACTS IN PROTEIN CRYSTALS

蛋白质晶体中堆积接触的分析

• 批准号: 3781258
• 负责人: S H BRYANT
• 金额: --
• 依托单位: NATIONAL LIBRARY OF MEDICINE
• 依托单位国家: 美国
• 资助国家: 美国
• 起止时间: 至
• 项目状态: 未结题
• 来源: https://reporter.nih.gov/project-details/3781258
• 关键词: chemical information system; intermolecular interaction; physical state; protein structure; statistics /biometry

The goal of this project is to identify common features of packing interactions in protein crystals, by statistical survey of structures in the Brookhaven Protein Data Bank. We have used functions in the PKB suite to identify a non-redundant subset of structures in the Protein Data Bank which have valid crystal symmetry information. For these structure we have tabulated crystal-packing contacts by residue and residue-pair type, and conducted statistical analyses. An interesting feature identified is the preferential participation of amino acids with small side chains, suggesting that lattice packing in diffraction-quality crystals must involve rigid intra-molecular contact of the polypeptide backbone. Another interesting feature is a clear correlation between the density of packing contacts and the resolution of available diffraction data, suggesting that lattice packing can reduce crystal disorder. The significance of this project is in providing a summary of protein-protein interactions as observed in crystals. These are very different from intra-molecular or oligomer-docking contacts, and they may provide a model for interactions expected in loosely-associated biological complexes.

这个项目的目标是确定包装的共同特点 蛋白质晶体中的相互作用， 布鲁克海文蛋白质数据库 我们使用了PKB中的函数 适用于识别蛋白质中结构的非冗余子集 具有有效晶体对称性信息的数据库。 为这些 结构我们按残基列出了晶体堆积接触， 残基配对类型，并进行统计分析。一个有趣 确定的特征是氨基酸的优先参与 小侧链，这表明晶格堆积在 衍射质量的晶体必须包含刚性的分子内接触 多肽骨架的一部分。 另一个有趣的特征是 堆积接触密度与分辨率的相关性 可用的衍射数据，表明晶格堆积可以 减少晶体无序。 该项目的意义在于 提供了蛋白质-蛋白质相互作用的总结， 晶体这些与分子内或 寡聚体对接接触，它们可以提供相互作用的模型 预期在松散相关的生物复合体中。