核ホルモン受容体におけるアロステリーと結合された配列の変異
1Howard Hughes Medical Institute, Departments of Molecular and Cell Biology and of Chemistry, University of California, Berkeley, CA 94707, USA.
Cell
|March 16, 2004
まとめ
関連するタンパク質の配列変化を分析すると,アロステル結合メカニズムが明らかになる. 核ホルモン受容体の変異は,これらの発見を確認し,RXR異体体におけるリガンド応答に影響を与えた.
科学分野:
- 分子生物学は分子生物学である.
- バイオケミストリー バイオケミストリー
- 進化生物学の進化生物学について
背景:
- 相関配列変異分析は,タンパク質の機能的な部位間のアロステル結合の洞察を提供します.
- 核ホルモン受容体は,これらのメカニズムを研究するための重要なタンパク質ファミリーです.
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Ligand Binding and Linkage
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 the...
Conserved Binding Sites
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 analyses the...
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 analyses the...
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About 48 different soluble family members of nuclear receptors are identified that can be divided into two main classes:
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