对Importinβ的Alphafold 3引导的洞察:Importin7的异构体相互作用及其与基因素H1的结合
Piotr Neumann1, Olexandr Dybkov2, Henning Urlaub3
1Department of Molecular Structural Biology, Institute for Microbiology and Genetics & GZMB, Georg-August-University Göttingen, 37077 Göttingen, Germany.
Structure (London, England : 1993)
|January 13, 2026
概括
进口因子7和进口因子β促进了H1基因组核的进口. 人工智能模型揭示了H1
科学领域:
- 分子生物学分子生物学
- 结构生物学 结构生物学
- 细胞生物学 细胞生物学
背景情况:
- 核进口的H1链接质子对于染色体组织至关重要.
- 这一过程由输送受体Importinβ (Impβ) 和Importin7 (Imp7) 的异构体介导.
- Impβ和Imp7之间的相互作用至关重要,涉及Imp7的C端残留物.
研究的目的:
- 阐明Impβ:Imp7:H1复合体形成的结构基础.
- 用实验数据验证人工智能驱动的结构预测.
- 了解Imp7的C端区域在进口过程中的作用.
主要方法:
- 关于Impβ:Imp7:H1复合物的AlphaFold3预测.
- 使用交叉连接,异热定位热量计和拉下测试进行验证.
- 根据冷电子显微镜数据对原子模型的改进.
主要成果:
- 产生了Impβ:Imp7:H1复合物的精确原子模型.
- H1球状域位于Imp7的中央腔内,而不是Impβ.
- Imp7的C端区域,包括具有FXFG动机的核类结合 (NlB) 区域,与Impβ相互作用.
结论:
- 这项研究为H1基因组核进口提供了高分辨率的结构模型.
- 人工智能驱动的预测,当与实验数据精细化时,提供准确的结构洞察力.
- Imp7在结合H1和通过其C端区域与Impβ相互作用方面发挥着直接作用.
关键词:
FG重复了一遍.H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H2 H1 H1 H1 H1 H2 H1 H3 H1 H1 H1 H1 H2 H1 H1 H1 H1 H1 H2 H1 H1 H1 H1 H2 H1 H1 H1 H1 H1 H2 H1 H1 H1 H2 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1 H1交叉链接 - 交叉链接核孔是一个核孔.核运输运输是核运输.核聚氨酸是核聚氨酸中的一种.更多相关视频
10:19Single-Molecule FRET Imaging for Observing the Conformational Dynamics of Dynamin-Like GTPase Atlastin
Published on: January 24, 2025
984
10:50Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography
Published on: March 9, 2010
17.9K
相关概念视频
Nuclear Localization Signals and Import
7.6K
Proteins targeted to the nucleus carry short stretches of amino acid sequences called the nuclear localization signal or NLS. Classical nuclear localization signals are of two types: monopartite and bipartite NLS. Monopartite classical NLS (cNLS) consists of a single cluster of 4-8 amino acids. Bipartite cNLS consists of two clusters of 2-3 amino acids and a 9-12 residue long proline-rich linker bridging the two clusters. Signal clusters are rich in positively charged amino acids such as...
7.6K
Nuclear Protein Sorting
6.2K
Nuclear protein sorting is the selective trafficking of histones, polymerases, gene regulatory proteins into the nucleus and exporting RNAs and ribosomes to the cytosol. It is a tightly controlled process that regulates gene expression within a cell.
Proteins targeted to the nucleus carry nuclear localization signals or NLS recognized by import receptors in the cytosol. Similarly, proteins with nuclear export signals are recognized by export receptors. Import and export receptors are...
Proteins targeted to the nucleus carry nuclear localization signals or NLS recognized by import receptors in the cytosol. Similarly, proteins with nuclear export signals are recognized by export receptors. Import and export receptors are...
6.2K
Nuclear Export
4.8K
The nucleus restricts several proteins within and allows others to pass. The restricted proteins possess a nuclear retention sequence or NRS, anchoring them to the nuclear lamins and preventing their transport to the cytosol. The non-restricted proteins, after their synthesis, are transported to their site of action, such as the cytosol or other organelles, with the help of nuclear export signals or NES.
NES are of three types- the canonical 10-residue long leucine-rich signal and other...
NES are of three types- the canonical 10-residue long leucine-rich signal and other...
4.8K
Mitochondrial Precursor Proteins
3.5K
Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70 chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial...
Most of the mitochondrial...
3.5K
Translocation of Proteins into the Mitochondria
12.1K
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
12.1K
Conserved Binding Sites
5.0K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
5.0K
