克拉特林光链LCA和LCB是相似的,多态的,并共享重复的七角形图案
概括
克拉特林轻链 (LCA和LCB) 密切相关,其结构特征表明它们在结合重链和其他蛋白质中的作用. 这解释了这些必不可少的细胞组成部分的组织特异性尺寸变化.
科学领域:
- 细胞生物学 细胞生物学
- 分子生物学分子生物学
- 蛋白质结构 蛋白质结构
背景情况:
- 克拉特林是一种蛋白质复合体,对囊泡形成至关重要.
- 克拉轻链 (LCA和LCB) 与克拉重链相结合.
- 已经观察到克拉特林轻链大小的特定组织变异.
研究的目的:
- 调查LCA和LCB类之间的关系.
- 为了阐明clathrin轻链功能的结构基础.
- 为了解释克拉特林光链中的取决于组织的大小变化.
主要方法:
- 来自老鼠大脑和肝脏的互补DNA克隆的分析.
- 氨基酸序列导出和分析.
主要成果:
- LCA和LCB类是密切相关的,有序相似之处.
- 每个类内的多个成员在保留位置上显示删除.
- 在序列的中央区域存在一个保存的alpha-helical卷轴-卷轴域.
- 氨基和炭基终端区域显示了蛋白质与蛋白质相互作用的潜力.
结论:
- 阿尔法螺旋段可能会调节结合克拉特林重链.
- 终端段涉及与其他蛋白质相互作用.
- 观察到的结构特征解释了克拉特林光链的组织特异性尺寸变化.
相关概念视频
Protein Complexes with Interchangeable Parts
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Lampbrush Chromosomes
In 1882, Flemming observed lampbrush chromosomes (LBC) in salamander eggs. Later in 1892, Rückert observed LBCs in shark egg cells and coined the term "lampbrush chromosomes" because they looked like brushes used to clean kerosene lamps.
LBCs are made up of two pairs of conjugating homologous chromatids. Each chromatid consists of alternatively positioned regions of condensed-inactive chromatin and loosely placed-active side loops, which can be contracted and extended. The loops resemble the...
LBCs are made up of two pairs of conjugating homologous chromatids. Each chromatid consists of alternatively positioned regions of condensed-inactive chromatin and loosely placed-active side loops, which can be contracted and extended. The loops resemble the...
COP Coated Vesicles
Membrane-enclosed structures called vesicles transport proteins and lipids across the cell. The vesicles derive their cargo from the plasma membrane, Golgi, ER, or endosome. Coated vesicles are spherical, protein-coated carriers with a 50–100 nm diameter that mediate bidirectional transport between the ER and the Golgi. The distribution of proteins between the ER and Golgi complex is dynamic and is maintained by different coated vesicles. Their formation is driven by the assembly of different...
Protein Complexes with Interchangeable Parts
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
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...


