ペレとチューブの死の領域の間の複合体の3次元構造

T Xiao¹, P Towb, S A Wasserman

¹The Howard Hughes Medical Institute and Department of Biochemistry, The University of Texas Southwestern Medical Center, Dallas 75235-9050, USA.

Cell

|December 10, 1999

まとめ

ペルとチューブタンパク質は,死領域を通じて相互作用し,ドーサルがドロソフィラの発達に不可欠な遺伝子発現を活性化することを可能にします. 構造と突然変異の分析は,この相互作用を確認しています.

科学分野:

発達生物学発達生物学とは
構造生物学構造生物学とは
分子生物学は分子生物学である.

背景:

セリン/スレオニンキナーゼペルとアダプタタンパク質チューブは,ドロソフィラの胚形成における重要な調節因子である.
彼らの相互作用は,ジゴティックパターン遺伝子を制御する転写因子であるDorsalの核転移に不可欠です.

研究の目的:

ペル・チューブ死亡領域相互作用の構造的基礎を解明する.
発達初期における背中の活性化と遺伝子発現の基礎となる分子メカニズムを理解する.

主な方法:

ヘテロジマー構造を決定するX線結晶学.
機能的有意性を評価するために,ペルとチューブ変異体を用いたインビボアッセイ.

主要な成果:

ペルとチューブの死亡ドメインは,6ヘリクスの束の折りたたみを持つヘテロダイマーを形成し,柔軟なインターフェイスで線形に配置されています.
挿入とC端尾を含むチューブ死亡領域の特定の構造的特徴は,ヘテロダイマー形成に不可欠です.
変異分析は,ヘテロジマーインターフェースの整合性が,ペルとチューブの in vivo 機能に不可欠であることを確認しました.

結論:

この研究は,ペル・チューブ・デス・ドメインの相互作用の原子の詳細を明らかにし,発達信号伝達経路の洞察を提供している.
この発見は,特定の構造要素と,タンパク質複合体の in vivo 機能のインタフェースの整合性の重要性を強調しています.

さらに関連する動画

08:00

DNA Nanotubes as a Versatile Tool to Study Semiflexible Polymers

Published on: October 25, 2017

7.2K

12:24

Helical Organization of Blood Coagulation Factor VIII on Lipid Nanotubes

Published on: June 3, 2014

12.7K

関連する概念動画

01:21

Structure of Porins

3.8K

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...

3.8K

01:09

Multi-pass Transmembrane Proteins and β-barrels

6.4K

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...

6.4K

01:25

Structure of Cadherins

4.6K

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...

4.6K

02:26

Conservation of Protein Domains Over Different Proteins

14.0K

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...

14.0K

02:21

Globular and Fibrous Proteins

46.7K

Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...

46.7K

02:15

Protein and Protein Structure

86.7K

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...