ダブルSの形状は,Dscamイソフォームの特別な結合特異性のための構造的基礎を提供します
Michael R Sawaya1, Woj M Wojtowicz, Ingemar Andre
1Howard Hughes Medical Institute, UCLA-DOE Institute of Genomics and Proteomics, Los Angeles, CA 90095, USA.
Cell
|September 23, 2008
まとめ
ドロソフィラ・DSCAMのタンパク質は,同位体特異の結合を通じて,正確な脳配線を確保する. 構造的研究は,変数と常数ドメインの相互作用が,この重要な細胞認識メカニズムをどのように可能にするかを明らかにします.
科学分野:
- 神経科学は神経科学である.
- 分子生物学は分子生物学である.
- 遺伝学 遺伝学とは
背景:
- ドロソフィラ・DSCAMのタンパク質は,広範囲にわたる同型多様性を生み出します.
- この多様性は,正確な神経回路形成に不可欠です.
- アイソフォームは,細胞認識に不可欠な特定の同性愛結合を示す.
研究 の 目的:
- Dscam アイソフォーム固有の同性愛結合の構造的基礎を解明する.
- ドロソフィラの脳における細胞認識の基礎となる分子機構を理解する.
主な方法:
- Dscamの構造を判別するX線結晶図 ((1-8).
- 結合相互作用を検証するための遺伝的および生化学的分析.
主要な成果:
- Dscam (((1-8) の構造は,S形の形状を持つ対称なホモジマーを示しています.
- この構造は,変数免疫グロブリンドメインの反並列"マッチング"を容易にする.
- 恒定ドメイン間の分子内相互作用も同性愛結合に寄与する.
結論:
- Dscamの同性愛結合特異性は,3つの変数Igドメインの"マッチング"から生じる.
- 内分子相互作用はホモダイマーを安定させ,結合特異性に寄与する.
- これらの発見は,DScam媒介の細胞認識を理解するための構造的枠組みを提供します.
関連する概念動画
Structure of Cadherins
5.0K
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...
5.0K
Assembly of Signaling Complexes
6.7K
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,...
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
6.7K
Conservation of Protein Domains Over Different Proteins
14.8K
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...
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
14.8K
Protein Complexes with Interchangeable Parts
3.0K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
3.0K
Single-Strand DNA Binding Proteins
16.9K
For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
16.9K
Antibody Structure
65.9K
Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
65.9K


