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関連する概念動画

Single-pass Transmembrane Proteins01:25

Single-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...
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-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...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Integrins01:10

Integrins

Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
Activation of Integrins01:15

Activation of Integrins

Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...

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Updated: May 7, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

基本的なアミノ酸のサイドチェーンは,トランスメブランのインテグリンシグナル伝達を調節する.

Chungho Kim1, Thomas Schmidt, Eun-Gyung Cho

  • 1Department of Medicine, University of California, San Diego, La Jolla, California 92093, USA.

Nature
|December 20, 2011
PubMed
まとめ
この要約は機械生成です。

スノーケリング残留物として知られる,膜インターフェースの近くにある陽性電荷のアミノ酸は,トランスメブラン領域 (TMD) の構造を維持し,細胞信号伝達を調節するために不可欠です. この研究では,インテグリンβ3TMD中のライシン716が,その地形と機能にどのように影響するか明らかにしています.

さらに関連する動画

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
12:05

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
09:14

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes

Published on: June 13, 2014

関連する実験動画

Last Updated: May 7, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
12:05

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
09:14

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes

Published on: June 13, 2014

科学分野:

  • バイオケミストリー バイオケミストリー
  • 構造生物学 構造生物学とは
  • 細胞シグナル伝達 細胞信号伝達

背景:

  • 膜界面のスノーケリング残留物 (ライシン/アルギニン側鎖) は,リン脂頭部群と相互作用することがあります.
  • 膜を越えた領域 (TMDs) でのシュノーケリングの機能的意義は,ほとんど未知のままです.
  • インテグリンβ-3TMDは,膜相互作用に関与する保存された基本的なアミノ酸を持っています.

研究 の 目的:

  • TMD トポグラフィの決定におけるインテグリンβ3ライシン716の役割を調査する.
  • インテグリンTMDによるトランスメブラン信号調節の構造的基礎を解明する.
  • スノーケリング残留物の変異がインテグリン機能にどのように影響するかを理解する.

主な方法:

  • 核磁気共鳴 (NMR) スペクトロスコーピーは,インテグリンアルファ-IIbベータ-3TMD.の構造を決定する.
  • サイト・ダイレクト・ミュータジェネシスで,ライシン716変異がTMD関連性およびインテグリン活性化に与える影響を評価する.
  • インテグリンの機能を回復する補償変異を特定するために,指向された進化.

主要な成果:

  • インテグリンβ3ライシン716はβ3TMDトポグラフィとα-IIbββ3TMD関連性を維持するために不可欠です.
  • ライシン716の変異は,TMD解離とインテグリン活性化につながる.
  • プロリン711を導入すると,TMDのキックが生じ,膜のクラップが解離され,インテグリンが不活性化されます.

結論:

  • シュノーケリングの残留物は,TMDの地形と膜の埋め込みを安定させる上で重要な役割を果たします.
  • シュノーケリング残留物の影響を受けた正確なTMD構造は,トランスメブラン信号伝達の調節に不可欠です.
  • この研究は,インテグリン活性化メカニズムと,膜タンパク質機能におけるスノーケリングのより広範な役割に関する構造的な洞察を提供します.