1B89

CLATHRIN HEAVY CHAIN PROXIMAL LEG SEGMENT (BOVINE)

1B89 の概要

• エントリーDOI: 10.2210/pdb1b89/pdb
• 分子名称: PROTEIN (CLATHRIN HEAVY CHAIN) (1 entity in total)
• 機能のキーワード: clathrin, triskelion, coated vesicles, endocytosis, self-assembly, alpha-alpha superhelix
• 由来する生物種: Bos taurus (cattle)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 52683.63

構造登録者

Ybe, J.A.,Brodsky, F.M.,Hofmann, K.,Lin, K.,Liu, S.-H.,Chen, L.,Earnest, T.N.,Fletterick, R.J.,Hwang, P.K. (登録日: 1999-05-27, 公開日: 1999-06-04, 最終更新日: 2024-10-30)

主引用文献

Ybe, J.A.,Brodsky, F.M.,Hofmann, K.,Lin, K.,Liu, S.H.,Chen, L.,Earnest, T.N.,Fletterick, R.J.,Hwang, P.K.
Clathrin self-assembly is mediated by a tandemly repeated superhelix.
Nature, 399:371-375, 1999

PubMed Abstract: Clathrin is a triskelion-shaped cytoplasmic protein that polymerizes into a polyhedral lattice on intracellular membranes to form protein-coated membrane vesicles. Lattice formation induces the sorting of membrane proteins during endocytosis and organelle biogenesis by interacting with membrane-associated adaptor molecules. The clathrin triskelion is a trimer of heavy-chain subunits (1,675 residues), each binding a single light-chain subunit, in the hub domain (residues 1,074-1,675). Light chains negatively modulate polymerization so that intracellular clathrin assembly is adaptor-dependent. Here we report the atomic structure, to 2.6 A resolution, of hub residues 1,210-1,516 involved in mediating spontaneous clathrin heavy-chain polymerization and light-chain association. The hub fragment folds into an elongated coil of alpha-helices, and alignment analyses reveal a 145-residue motif that is repeated seven times along the filamentous leg and appears in other proteins involved in vacuolar protein sorting. The resulting model provides a three-dimensional framework for understanding clathrin heavy-chain self-assembly, light-chain binding and trimerization.

PubMed: 10360576
DOI: 10.1038/20708

実験手法

X-RAY DIFFRACTION (2.6 Å)