7SC0

CryoEM structure of the Caveolin-1 8S complex

7SC0 の概要

• エントリーDOI: 10.2210/pdb7sc0/pdb
• EMDBエントリー: 25007
• 分子名称: Caveolin-1 (1 entity in total)
• 機能のキーワード: caveolin, caveolae, cryoem, disc, monotopic proteins, structural protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 11
• 化学式量合計: 225440.34

構造登録者

Porta, J.P.,Ohi, M.D.,Kenworthy, A.K.,Karakas, E. (登録日: 2021-09-26, 公開日: 2022-05-25, 最終更新日: 2024-06-05)

主引用文献

Porta, J.C.,Han, B.,Gulsevin, A.,Chung, J.M.,Peskova, Y.,Connolly, S.,Mchaourab, H.S.,Meiler, J.,Karakas, E.,Kenworthy, A.K.,Ohi, M.D.
Molecular architecture of the human caveolin-1 complex.
Sci Adv, 8:eabn7232-eabn7232, 2022

PubMed Abstract: Membrane-sculpting proteins shape the morphology of cell membranes and facilitate remodeling in response to physiological and environmental cues. Complexes of the monotopic membrane protein caveolin function as essential curvature-generating components of caveolae, flask-shaped invaginations that sense and respond to plasma membrane tension. However, the structural basis for caveolin's membrane remodeling activity is currently unknown. Here, we show that, using cryo-electron microscopy, the human caveolin-1 complex is composed of 11 protomers organized into a tightly packed disc with a flat membrane-embedded surface. The structural insights suggest a previously unrecognized mechanism for how membrane-sculpting proteins interact with membranes and reveal how key regions of caveolin-1, including its scaffolding, oligomerization, and intramembrane domains, contribute to its function.

PubMed: 35544577
DOI: 10.1126/sciadv.abn7232

実験手法

ELECTRON MICROSCOPY (3.4 Å)