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1b89
From Proteopedia
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[[Image:1b89.gif|left|200px]] | [[Image:1b89.gif|left|200px]] | ||
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'''CLATHRIN HEAVY CHAIN PROXIMAL LEG SEGMENT (BOVINE)''' | '''CLATHRIN HEAVY CHAIN PROXIMAL LEG SEGMENT (BOVINE)''' | ||
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[[Category: Liu, S H.]] | [[Category: Liu, S H.]] | ||
[[Category: Ybe, J A.]] | [[Category: Ybe, J A.]] | ||
| - | [[Category: | + | [[Category: Alpha-alpha superhelix]] |
| - | [[Category: | + | [[Category: Clathrin]] |
| - | [[Category: | + | [[Category: Coated vesicle]] |
| - | [[Category: | + | [[Category: Endocytosis]] |
| - | [[Category: | + | [[Category: Self-assembly]] |
| - | [[Category: | + | [[Category: Triskelion]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:11:41 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 08:11, 2 May 2008
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 Page seeded by OCA on Fri May 2 11:11:41 2008
