ANALYSIS OF PACKING CONTACTS IN PROTEIN CRYSTALS

蛋白质晶体中堆积接触的分析

• 批准号: 3759296
• 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/3759296
• 关键词: X ray crystallography; chemical information system; chemical models; 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 indeed reduce crystal disorder. Significance to Biomedical Research: 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通过结构的统计调查， 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， 小的侧链，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 确实减少了晶体无序。 对生物医学研究的意义： 该项目的意义在于提供一个总结， 在晶体中观察到的蛋白质-蛋白质相互作用。这些都是非常 不同于分子内或寡聚体对接接触，并且它们 可以提供一个模型的相互作用预期在松散关联 生物复合体