1b89

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|PDB= 1b89 |SIZE=350|CAPTION= <scene name='initialview01'>1b89</scene>, resolution 2.60&Aring;
|PDB= 1b89 |SIZE=350|CAPTION= <scene name='initialview01'>1b89</scene>, resolution 2.60&Aring;
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b89 OCA], [http://www.ebi.ac.uk/pdbsum/1b89 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b89 RCSB]</span>
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[[Category: triskelion]]
[[Category: triskelion]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:55:38 2008''

Revision as of 15:55, 30 March 2008


PDB ID 1b89

Drag the structure with the mouse to rotate
, resolution 2.60Å
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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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