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Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

11.8K
Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
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Ligand Binding Sites02:40

Ligand Binding Sites

11.9K
Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
11.9K
Conserved Binding Sites01:49

Conserved Binding Sites

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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...
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Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
4.4K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

12.1K
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
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Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

4.7K
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,...
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Updated: May 2, 2026

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

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14-3-3の構造的基礎は,フォスホペプチド結合特異性である

M B Yaffe1, K Rittinger, S Volinia

  • 1Department of Medicine, Beth Israel Deaconess Medical Center, Boston, Massachusetts 02215, USA.

Cell
|January 15, 1998
PubMed
まとめ
この要約は機械生成です。

研究者らは,細胞シグナル伝達に不可欠な14-3-3タンパク質ファミリーの2つの重要な結合モチーフ (RSXpSXPとRXY/FXpSXP) を特定しました. これらの発見は,14-3-3タンパク質が他の分子とどのように相互作用するかを明らかにします.

さらに関連する動画

PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions
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PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions

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Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
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関連する実験動画

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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
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PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions
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Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
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科学分野:

  • 分子生物学は分子生物学である.
  • タンパク質の生化学
  • 細胞シグナル伝達 細胞信号伝達

背景:

  • 14-3-3タンパク質ファミリーは,信号伝達経路を媒介する上で重要な役割を果たします.
  • これらのタンパク質は,特定のフォスフォセリンを含む標的タンパク質に結合することで機能します.
  • これらの相互作用を理解することは,セルラー通信ネットワークの解読の鍵です.

研究 の 目的:

  • 14-3-3タンパク質ファミリーによって認識される結合モチーフを特定し,特徴づけること.
  • 14-3-3タンパク質-リガンド相互作用の構造的基礎を解明する.
  • 細胞信号伝達機構におけるこれらの相互作用の影響を調査する.

主な方法:

  • 哺乳類および酵母14-3-3タンパク質を検出するために,フォスフォセリン指向ペプチドライブラリを使用しました.
  • フォスフォセリンのモチーフを持つ14-3-3ゼータ複合体の結晶構造を決定しました.
  • 結晶構造内のペプチドとタンパク質の相互作用を分析した.

主要な成果:

  • 2つの主要な14-3-3結合モチーフ,RSXpSXPとRXY/FXpSXPを特定しました.
  • 14-3-3zeta複合体の特定のペプチド構成が観察され,シス構成のプロリン残留が含まれています.
  • 14-3-3ジマーがタンデムフォスホセリンのモチーフに結合することを実証し,バイデント結合機構を示唆した.

結論:

  • 特定されたモチーフは,既知の14-3-3結合タンパク質に多く見られます.
  • 構造データは,観察されたペプチドライブラリ結果の分子基礎を提供します.
  • タンデムモチーフとのバイデントアソシエーションは,Raf,BAD,Cbl.のようなタンパク質にとって重要なシグナル伝達メカニズムを表しています.