1b89
From Proteopedia
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CLATHRIN HEAVY CHAIN PROXIMAL LEG SEGMENT (BOVINE)
Overview
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.
About this Structure
1B89 is a Single protein structure of sequence from Bos taurus. The following page contains interesting information on the relation of 1B89 with [Clathrin]. Full crystallographic information is available from OCA.
Reference
Clathrin self-assembly is mediated by a tandemly repeated superhelix., Ybe JA, Brodsky FM, Hofmann K, Lin K, Liu SH, Chen L, Earnest TN, Fletterick RJ, Hwang PK, Nature. 1999 May 27;399(6734):371-5. PMID:10360576
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