由CALHM2和CALHM4对应物组成的异构管道的结构特征
Katarzyna Drożdżyk1, Martina Peter1, Raimund Dutzler1
1Department of Biochemistry, University of Zurich, Zurich, Switzerland.
eLife
|June 19, 2024
概括
这项研究揭示了胎盘CALHM2和CALHM4蛋白如何形成异构管道. 这些CALHM异构体以特定的固态度和子单元排列组合在一起,为其细胞功能提供了洞察力.
科学领域:
- 生物化学 生物化学
- 分子生物学分子生物学
- 膜蛋白研究研究 膜蛋白研究
背景情况:
- 平衡和黑色素瘤 (CALHM) 蛋白质家族包括六种人类类型,形成大型毛孔通道.
- 已知CALHM1和CALHM3在味觉中调解ATP释放,形成由特定条件激活的异构管道.
- CALHM2,CALHM4和CALHM6在胎盘中高度表达,它们的通道特性和组合特征基本上没有特征.
研究的目的:
- 为了研究胎盘CALHM类似物,特别是CALHM2和CALHM4.4的异构组合.
- 描述CALHM2/CALHM4异构复合物的结构性质和固体几何学.
- 了解这些异构体通道内的子单元的构造状态.
主要方法:
- 使用特定的结合物作为信托标记来识别和表征CALHM2和CALHM4异构体.
- 分析了由CALHM2和CALHM4.4形成的异构体复合物的组装固体几何学.
- 检查了组装的异构体通道内的子单元的构造分离.
主要成果:
- CALHM2和CALHM4蛋白质组合成具有不同固态度的异构复合体.
- 异构体复合体的主要群体显示CALHM2是主要组成部分.
- 在这些寡合体中,CALHM子单元分离,采用与它们的同质道状态相一致的构造.
结论:
- CALHM2和CALHM4形成异构管道,具有独特的结构和固体测量特性.
- 在CALHM异构体内的子单元分离会影响它们的结构状态.
- CALHM异构体的形成和特性对细胞功能具有重要意义,特别是在胎盘组织中.
更多相关视频
07:47A Proteoliposome-Based Efflux Assay to Determine Single-molecule Properties of Cl- Channels and Transporters
Published on: April 20, 2015
9.8K
08:54Monitoring Leucine-Rich Repeat Containing 8 Channel (LRRC8/VRAC) Activity Using Sensitized-Emission Förster Resonance Energy Transfer (SE-FRET)
Published on: August 9, 2024
418
相关概念视频
Multi-pass Transmembrane Proteins and β-barrels
5.3K
In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
5.3K
Structure of Cadherins
3.3K
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...
3.3K
Calmodulin-dependent Signaling
5.1K
Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
5.1K
Gap Junctions
8.0K
The cytoplasm of adjacent animal cells can exchange small molecules, ions, and secondary messengers via the communication channels which form the gap junctions. These junctions comprise a few hundred to thousands of molecular channels, each made of two halves, called the connexon hemichannel. A connexon is a hexamer of six transmembrane connexin proteins, which assemble radially, thus forming a pore or channel in the center. One connexon hemichannel docks with a corresponding connexon on the...
8.0K
Ligand-gated Ion Channels
12.4K
Ligand-gated ion channels are transmembrane proteins with a channel for ions to pass through and a binding site for a ligand. The channel opens only when a ligand attaches to the binding site.
Three Subfamilies of Ligand-gated Ion Channels
Ligand-gated ion channels fall into three subfamilies. The 'Cys-loop' includes the nicotinic acetylcholine receptors, γ-aminobutyric acid (GABA), glycine, and 5-hydroxytryptamine receptors. The second one is the 'Pore-loop' channels that...
Three Subfamilies of Ligand-gated Ion Channels
Ligand-gated ion channels fall into three subfamilies. The 'Cys-loop' includes the nicotinic acetylcholine receptors, γ-aminobutyric acid (GABA), glycine, and 5-hydroxytryptamine receptors. The second one is the 'Pore-loop' channels that...
12.4K
Aquaporins
4.8K
Aquaporins or AQPs are a family of integral membrane proteins whose primary function is to transport water, while some called aquaglyceroporins also transport glycerol. In addition, aquaporins have also been suspected to be involved in transporting volatile substances, such as carbon dioxide and ammonia, across membranes. Such AQPs that act as gas channels are often highly expressed in cells involved in the gaseous exchange, such as red blood cells, epithelial cells, and pulmonary capillaries.
4.8K
