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Updated: May 19, 2026
06:45
Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
Published on: May 26, 2011
宿主膜によって支配されるトランスメブランの螺旋型タンパク質二重体の多州組織である
Anton A Polyansky1, Pavel E Volynsky, Roman G Efremov
1Department of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, Vienna, AT-1030, Austria. newant@gmail.com
Journal of the American Chemical Society
|August 15, 2012
まとめ
細胞膜におけるトランスメブランヘリックス二酸化は,タンパク質の機能にとって極めて重要です. 私たちの計算モデルは,膜環境がダイマー構成と安定性にどのように影響し,ErbBのダイメリゼーションの強さを腫瘍学的可能性と結びつけるかを明らかにします.
科学分野:
- バイオフィジックス 生物物理学
- コンピュータ生物学 コンピュータ生物学
- 構造生物学 構造生物学とは
背景:
- トランスメンブレーン (TM) ヘリックス結合は,ビトピックタンパク質の機能,特にレセプターチロシンキナーゼ (RTKs) のために不可欠であり,これらは重要な医学的標的である.
- TMヘリックス二分化の理解は,主構造,膜組成,局所環境などの要因により複雑である.
研究 の 目的:
- ビトピックタンパク質のTMヘリカルホモおよびヘテロディメリゼーションを分析するためのコンピューティングフレームワークを開発し,適用する.
- TM二元体の形状と安定性に対する膜環境の影響を調査する.
主な方法:
- TMダイマー構成を予測するための新しい表面ベースのモデリングアプローチを開発しました.
- 様々なモデル膜で全原子分子ダイナミクスシミュレーションを行い,ダイマーの振る舞いを研究した.
- 形状的異質性および環境の影響が二分化に及ぼす影響を分析した.
主要な成果:
- コンピューティングフレームワークは,TMダイマー構成を正確に予測し,構成異質性をスクリーン化します.
- 特定の脂質二重層は,タンパク質構造と膜の相互作用に基づいて,異なる二重体構成を好ましく安定させます.
- タンパク質によって引き起こされる膜の乱れは,自由エネルギー獲得への膜の貢献と相関する.
結論:
- 細胞膜の環境は,特定のTMダイマー構造の選択において重要な役割を果たします.
- ErbBファミリー内のダイメリゼーション強度は,がん発生能力と相関しており,がんのメカニズムに関する洞察を提供します.
関連する概念動画
01:09Multi-pass Transmembrane Proteins and β-barrels
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 G-protein-linked receptors (GPCRs) and...
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
01:29Insertion of Multi-pass Transmembrane Proteins in the RER
The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
01:25Single-pass Transmembrane Proteins
Integral membrane proteins are tightly associated with the cell membrane and play a crucial role in cell communication, signaling, adhesion, and transport of the molecules. Some integral membrane proteins are present only in the membrane monolayer. For example, the enzyme fatty acid amide hydrolase is present in the cytoplasmic side of the membrane monolayer. In contrast, another type of integral membrane protein, also known as a transmembrane protein, spans across the membrane. Transmembrane...
00:59Mechanisms 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...
01:21Structure of Porins
Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel precursors...
01:26Insertion of Single-pass Transmembrane Proteins in the RER
Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...