晶体结构在2.2 A分辨率上,从人体动力中得到了斑块同质域的分辨率
K M Ferguson1, M A Lemmon, J Schlessinger
1Department of Molecular Biophysics and Biochemistry, Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06510.
Cell
|October 21, 1994
概括
人类动力素斑链同质性 (PH) 域结构揭示了一个保存的折叠. 这种由X射线晶体学确定的结构突出显示了一个带正电荷的表面,可能参与了连接体结合.
科学领域:
- 结构生物学 结构生物学
- 生物化学 生物化学
- 分子动力学分子动力学
背景情况:
- 斑蛋白同质 (PH) 域是一个关键的蛋白质模块,参与各种细胞过程.
- 了解PH域功能的结构基础对于破译蛋白质-蛋白质相互作用和信号通路至关重要.
研究的目的:
- 为了确定人类动力素斑同质 (PH) 域的高分辨率X射线晶体结构.
- 阐明胺PH域的结构特征和潜在的功能影响.
主要方法:
- 采用X射线晶体学,将人类动氨酸PH域的结构精细化至2.2A分辨率.
- 进行了与其他已知的PH域进行比较的结构分析.
主要成果:
- 精致的结构揭示了一个保存的七链β三明治折叠,由C端α螺旋环关闭.
- 三个可变循环形成一个独特的正电荷表面,在PH域中保持.
- 这种带电的表面可以作为连接物结合点,并包括与X相关免疫缺陷相关的已知突变的位置.
结论:
- 人类动氨酸PH域与其他PH域共享一个保存的结构折叠.
- 确定的正电荷表面是关键特征,表明它在连接体识别中的作用,并可能与疾病突变有关.
- 这种结构的洞察力为进一步的功能研究提供了基础.
相关概念视频
X-ray Crystallography
The size of the unit cell and the arrangement of atoms in a crystal may be determined from measurements of the diffraction of X-rays by the crystal, termed X-ray crystallography.
Diffraction
Diffraction is the change in the direction of travel experienced by an electromagnetic wave when it encounters a physical barrier whose dimensions are comparable to those of the wavelength of the light. X-rays are electromagnetic radiation with wavelengths about as long as the distance between neighboring...
Diffraction
Diffraction is the change in the direction of travel experienced by an electromagnetic wave when it encounters a physical barrier whose dimensions are comparable to those of the wavelength of the light. X-rays are electromagnetic radiation with wavelengths about as long as the distance between neighboring...
ATP Synthase: Structure
ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
Pinching-off of Coated Vesicles
Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
Mechanisms of Membrane Domain Formation
Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
Clathrin Coated Vesicles
Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
Structure of Cadherins
The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins” is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This diversity of cadherins...


