1BPO

CLATHRIN HEAVY-CHAIN TERMINAL DOMAIN AND LINKER

1BPO の概要

• エントリーDOI: 10.2210/pdb1bpo/pdb
• 分子名称: PROTEIN (CLATHRIN) (2 entities in total)
• 機能のキーワード: clathrin endocytosis beta-propeller coated-pits, membrane protein
• 由来する生物種: Rattus norvegicus (Norway rat)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 165270.50

構造登録者

Harr, E.T.,Musacchio, A.,Harrison, S.C.,Kirchhausen, T. (登録日: 1998-08-11, 公開日: 1998-12-16, 最終更新日: 2023-12-27)

主引用文献

Haar, E.T.,Musacchio, A.,Harrison, S.C.,Kirchhausen, T.
Atomic structure of clathrin: a beta propeller terminal domain joins an alpha zigzag linker.
Cell(Cambridge,Mass.), 95:563-573, 1998

PubMed Abstract: Clathrin triskelions form the lattice that organizes recruitment of proteins to coated pits and helps drive vesiculation of the lipid bilayer. We report the crystal structure at 2.6 A resolution of a 55 kDa N-terminal fragment from the 190 kDa clathrin heavy chain. The structure comprises the globular "terminal domain" and the linker that joins it to the end of a triskelion leg. The terminal domain is a seven-blade beta propeller, a structure well adapted to interaction with multiple partners, such as the AP-1 and AP-2 sorting adaptor complexes and the nonvisual arrestins. The linker is an alpha-helical zigzag emanating from the propeller domain. We propose that this simple motif may extend into the rest of the clathrin leg.

PubMed: 9827808
DOI: 10.1016/S0092-8674(00)81623-2

実験手法

X-RAY DIFFRACTION (2.6 Å)