4QKW

Crystal structure of the zebrafish cavin4a HR1 domain

4QKW の概要

• エントリーDOI: 10.2210/pdb4qkw/pdb
• 関連するPDBエントリー: 4QKV
• 分子名称: Muscle-related coiled-coil protein, CHLORIDE ION (3 entities in total)
• 機能のキーワード: coiled-coil, signalling, plasma membrane, signaling protein
• 由来する生物種: Danio rerio (leopard danio,zebra danio,zebra fish)
• 細胞内の位置: Cytoplasm, myofibril, sarcomere : A1L260
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 36584.22

構造登録者

Kovtun, O.,Tillu, V.,Parton, R.G.,Collins, B.M. (登録日: 2014-06-10, 公開日: 2015-03-18, 最終更新日: 2024-03-20)

主引用文献

Kovtun, O.,Tillu, V.A.,Jung, W.,Leneva, N.,Ariotti, N.,Chaudhary, N.,Mandyam, R.A.,Ferguson, C.,Morgan, G.P.,Johnston, W.A.,Harrop, S.J.,Alexandrov, K.,Parton, R.G.,Collins, B.M.
Structural insights into the organization of the cavin membrane coat complex
Dev.Cell, 31:405-419, 2014

PubMed Abstract: Caveolae are cell-surface membrane invaginations that play critical roles in cellular processes including signaling and membrane homeostasis. The cavin proteins, in cooperation with caveolins, are essential for caveola formation. Here we show that a minimal N-terminal domain of the cavins, termed HR1, is required and sufficient for their homo- and hetero-oligomerization. Crystal structures of the mouse cavin1 and zebrafish cavin4a HR1 domains reveal highly conserved trimeric coiled-coil architectures, with intersubunit interactions that determine the specificity of cavin-cavin interactions. The HR1 domain contains a basic surface patch that interacts with polyphosphoinositides and coordinates with additional membrane-binding sites within the cavin C terminus to facilitate membrane association and remodeling. Electron microscopy of purified cavins reveals the existence of large assemblies, composed of a repeating rod-like structural element, and we propose that these structures polymerize through membrane-coupled interactions to form the unique striations observed on the surface of caveolae in vivo.

PubMed: 25453557
DOI: 10.1016/j.devcel.2014.10.002

実験手法

X-RAY DIFFRACTION (1.7 Å)