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)''' | + | {{Structure |
| + | |PDB= 1b89 |SIZE=350|CAPTION= <scene name='initialview01'>1b89</scene>, resolution 2.60Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CLATHRIN HEAVY CHAIN PROXIMAL LEG SEGMENT (BOVINE)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1B89 is a [ | + | 1B89 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. The following page contains interesting information on the relation of 1B89 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb88_1.html Clathrin]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B89 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10360576 10360576] |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Clathrin]] | [[Category: Clathrin]] | ||
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[[Category: alpha-alpha superhelix]] | [[Category: alpha-alpha superhelix]] | ||
[[Category: clathrin]] | [[Category: clathrin]] | ||
| - | [[Category: coated | + | [[Category: coated vesicle]] |
[[Category: endocytosis]] | [[Category: endocytosis]] | ||
[[Category: self-assembly]] | [[Category: self-assembly]] | ||
[[Category: triskelion]] | [[Category: triskelion]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:07:36 2008'' |
Revision as of 08:07, 20 March 2008
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| , resolution 2.60Å | |||||||
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| 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
Page seeded by OCA on Thu Mar 20 10:07:36 2008
