ENZYME ACTIVE SITE TEMPLATES

酶活性位点模板

• 批准号: 8170507
• 负责人: PATRICIA CLEMENT BABBITT
• 金额: $ 1.79万
• 依托单位: UNIVERSITY OF CALIFORNIA, SAN FRANCISCO
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-07-01 至 2011-06-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8170507
• 关键词: Active Sites; Architecture; Bioinformatics; Chimera organism; Computer Retrieval of Information on Scientific Projects Database; Computer software; Development; Diagnostic; Enzymes; Family; Funding; Goals; Grant; Institution; Methods; Proteins; Publishing; Research; Research Personnel; Resources; Source; Structure; United States National Institutes of Health; Work; base; enolase; haloacid dehalogenase; tool; web site

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The Babbitt group has been a pioneer in identifying enzyme superfamilies, that is, groups of proteins that are distantly evolutionarily related and share nearly undetectable sequence similarity, but that share an architecture and certain aspects of their function. We are comparing structures and observables based on structure among and between families and superfamilies of proteins, with the goal of better understanding how sequence and structure are constrained. We are identifying 3D motifs or active site templates, spatial arrangements of small sets of residues that can be diagnostic of membership in a family or superfamily of proteins. Besides studying known superfamilies, we also wish to characterize sets of related proteins that have not already been well described. Chimera and other sequence and structure analysis tools available locally and on the RBVI web site are employed in this work. We collaborate with the Chimera development team as needed to further the research and facilitate the creation of useful research software. Our initial work on active site templates for the enolase and haloacid dehalogenase superfamilies has been published in Proteins (see below). More recently, our method to automatically discover 3D motifs shared among any group of related proteins has been published in Bioinformatics.

该副本是利用众多研究子项目之一 由NIH/NCRR资助的中心赠款提供的资源。子弹和 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此可以在其他清晰的条目中代表。列出的机构是 对于中心，这不一定是调查员的机构。 巴比特集团一直是识别酶超家族的先驱， 也就是说，在进化上相关的一组蛋白质和 共享几乎无法检测到的序列相似性，但该序列具有架构及其功能的某些方面。 我们正在比较基于蛋白质家庭和超家族之间结构的结构和可观察物，目的是更好地了解序列和结构如何受到约束。 我们正在确定3D主题或活动现场模板，可以诊断为家庭或蛋白质超家族的少量残基的空间排列。 除了研究已知的超家族外，我们还希望表征尚未得到很好描述的相关蛋白质集。 嵌合体以及其他序列和结构分析工具本地可用，在RBVI网站上可用。 我们根据需要与Chimera Development团队合作，以进一步进行研究并促进创建有用的研究软件。 我们在烯醇酶和卤素的活动现场模板上的最初工作 脱核酶超家族已发表在蛋白质中（见下文）。最近，我们在生物信息学中发表的任何相关蛋白质中共享的3D基序的方法已在生物信息学中发表。