由整体旋转扩散张力指导的多域蛋白质和蛋白质复合体的结构组合
Yaroslav Ryabov1, David Fushman
1Department of Chemistry and Biochemistry, Center for Biomolecular Structure and Organization, University of Maryland, College Park, Maryland 20742, USA.
Journal of the American Chemical Society
|June 7, 2007
概括
这项研究引入了一种使用蛋白质的旋转扩散张量来精确定位复杂蛋白质结构中的域的新方法. 这一进步提高了利用NMR放松数据在溶液中蛋白质的结构特征.
科学领域:
- 结构生物学 结构生物学
- 生物物理学的生物物理.
- 计算生物学 计算生物学
背景情况:
- 确定多域蛋白和蛋白质复合体内域的精确排列对于理解它们的功能至关重要.
- 现有的域位定位方法往往面临局限性,特别是对于具有显著域移动性的系统.
研究的目的:
- 开发一种新的,强大的方法来限制多域蛋白和蛋白质-蛋白质复合体中的域定位.
- 为了利用从NMR放松数据中获得的整体旋转扩散张力,进行详细的结构特征.
- 为了能够准确地确定具有动态域运动的系统的结构,包括不同的构造状态.
主要方法:
- 利用旋转扩散张量的两个主要轴和主要值.
- 开发一种算法,以找到最符合实验扩散张量数据的域排列.
- 通过已知的蛋白质系统 (HIV-1蛋白酶同位体,马尔托结合蛋白) 和模拟数据验证方法.
主要成果:
- 对于具有已知的结构的系统,在定位域中证明了准确性.
- 成功确定了Lys48连接二维基因链的开放和闭合构造的结构,克服了其他方法的局限性.
- 通过计算测试展示了该方法对域定位的敏感性.
结论:
- 拟议的方法为溶液中的蛋白质的结构特征提供了一个强大的新工具.
- 它扩展了NMR放松数据的实用性,用于分析复杂的多域蛋白及其相互作用.
- 开辟了研究蛋白质动力学和域级结构变化的新途径.
相关概念视频
Protein Folding
Overview
Protein Folding
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Complex Assembly
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complex Assembly
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Diffusion in the Membrane
Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
Assembly of Signaling Complexes
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...


