リンクモジュールの溶液構造:細胞外マトリックス安定性と細胞移動に関与するヒアルロン結合ドメイン
D Kohda1, C J Morton, A A Parkar
1Department of Biochemistry Oxford Centre for Molecular Sciences University of Oxford, United Kingdom.
Cell
|September 6, 1996
まとめ
細胞外マトリックスタンパク質のヒアルロナンの結合ドメインであるリンクモジュールは,定義された構造を持っています. この構造は,ヒアルロノンと相互作用し,C型レクチン領域との類似性を明らかにします.
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
- 細胞外マトリックス研究
背景:
- リンクモジュールは,細胞外マトリックス組立,細胞結合,および移動に不可欠なタンパク質の重要なヒアルロナンの結合ドメインです.
- これらのドメインの構造を理解することは,生物学的プロセスにおけるそれらの機能を明らかにする鍵です.
研究 の 目的:
- 人間のTSG-6からリンクモジュールの溶液構造を決定する.
- TSG-6 Link モジュールのヒアルロナンの結合表面を特定するために.
- リンクモジュールの構造を他の既知のタンパク質ドメインと比較するために.
主な方法:
- 溶液構造の決定のための核磁気共鳴 (NMR) スペクトロスコーピー.
- バイオインフォマティック構造データベース検索.
主要な成果:
- ヒトのTSG-6リンクモジュールの溶液構造を決定し,2つのアルファヘリクと2つの反パラレルベータシートを持つ折り畳みを明らかにしました.
- TSG-6リンクモジュールで,仮の hialuronan 結合表面が特定されました.
- LinkモジュールはC型レクチンドメインと構造的に類似しており,ヒアルロナンの結合部位はE-セレクチンの炭水化物結合部位に類似しています.
結論:
- 決定された構造は,CD44,軟骨結合タンパク質,およびaggrecan.canを含むLinkモジュールスーパーファミリーのコンセンサスフォールドを表しています.
- この発見は,Linkモジュールによるヒアルロナンの結合の分子基礎についての洞察を提供します.
- 構造的な類似性は,リンクモジュールとC型レクチン間の潜在的機能的重複や進化的関係を示唆する.
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