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Powder Diffraction Methods for Membrane Protein Structure Determination

用于膜蛋白结构测定的粉末衍射方法

基本信息

批准号：
BB/J020702/1
负责人：
Bonnie Wallace
金额：
$ 14.95万
依托单位：
Birkbeck, University of London
依托单位国家：
英国
项目类别：
Research Grant
财政年份：
2012
资助国家：
英国
起止时间：
2012 至无数据
项目状态：
已结题

来源：
https://gtr.ukri.org/projects?ref=BB%2FJ020702%2F1
关键词：
Powder Diffraction Methods Membrane Protein

项目摘要

Membrane proteins comprise a large proportion of all the proteins coded by human and other eukaryotic genomes, and are the targets of more than one-half of all the pharmaceutical drugs marketed today. Knowledge of their three-dimensional structure is important for understanding how they function, and for the development of new drugs for the treatment of diseases. Protein X-ray crystallographic studies, which require well-ordered, large single crystals of the protein, provide such structural information. However, one of the major obstacles to membrane protein structure determinations currently is the ability to produce crystals of a size and quality suitable for single crystal studies. Although often many much smaller crystals can be produced, there has yet to be a method developed to utilise these for the determination of the structure of membrane proteins. The aim of this project is to develop both the methodology and tools necessary to determine the structure of membrane proteins based on samples not of single crystals, but of bunches of very small (microcrystals) using powder diffraction techniques.

膜蛋白构成了人类和其他真核生物基因组编码的所有蛋白质的很大一部分，并且是当今市场上一半以上的药物的靶标。了解它们的三维结构对于理解它们的功能和开发治疗疾病的新药非常重要。蛋白质x射线晶体学研究提供了这样的结构信息，这需要蛋白质的有序、大的单晶。然而，目前膜蛋白结构测定的主要障碍之一是制备适合单晶研究的尺寸和质量的晶体的能力。虽然通常可以生产出许多更小的晶体，但还没有开发出一种方法来利用这些晶体来确定膜蛋白的结构。该项目的目的是开发必要的方法和工具，以确定膜蛋白的结构基于样品，而不是单晶，但束非常小（微晶体）使用粉末衍射技术。

项目成果

期刊论文数量（7）

专著数量（0）

科研奖励数量（0）

会议论文数量（0）

专利数量（0）

Role of the C-terminal domain in the structure and function of tetrameric sodium channels.

DOI：
10.1038/ncomms3465
发表时间：
2013
期刊：
NATURE COMMUNICATIONS
影响因子：
16.6
作者：
Bagneris, Claire;DeCaen, Paul G.;Hall, Benjamin A.;Naylor, Claire E.;Clapham, David E.;Kay, Christopher W. M.;Wallace, B. A.
通讯作者：
Wallace, B. A.

Structure of a bacterial voltage-gated sodium channel pore reveals mechanisms of opening and closing.