1b89
From Proteopedia
(New page: 200px<br /> <applet load="1b89" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b89, resolution 2.60Å" /> '''CLATHRIN HEAVY CHAI...) |
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| - | [[Image:1b89.gif|left|200px]]<br /> | + | [[Image:1b89.gif|left|200px]]<br /><applet load="1b89" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1b89" size=" | + | |
caption="1b89, resolution 2.60Å" /> | caption="1b89, resolution 2.60Å" /> | ||
'''CLATHRIN HEAVY CHAIN PROXIMAL LEG SEGMENT (BOVINE)'''<br /> | '''CLATHRIN HEAVY CHAIN PROXIMAL LEG SEGMENT (BOVINE)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Clathrin is a triskelion-shaped cytoplasmic protein that polymerizes into | + | 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== | ==About this Structure== | ||
| - | 1B89 is a [http://en.wikipedia.org/wiki/Single_protein 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:// | + | 1B89 is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: Clathrin]] | [[Category: Clathrin]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Brodsky, F | + | [[Category: Brodsky, F M.]] |
[[Category: Chen, L.]] | [[Category: Chen, L.]] | ||
| - | [[Category: Earnest, T | + | [[Category: Earnest, T N.]] |
| - | [[Category: Fletterick, R | + | [[Category: Fletterick, R J.]] |
[[Category: Hofmann, K.]] | [[Category: Hofmann, K.]] | ||
| - | [[Category: Hwang, P | + | [[Category: Hwang, P K.]] |
[[Category: Lin, K.]] | [[Category: Lin, K.]] | ||
| - | [[Category: Liu, S | + | [[Category: Liu, S H.]] |
| - | [[Category: Ybe, J | + | [[Category: Ybe, J A.]] |
[[Category: alpha-alpha superhelix]] | [[Category: alpha-alpha superhelix]] | ||
[[Category: clathrin]] | [[Category: clathrin]] | ||
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[[Category: triskelion]] | [[Category: triskelion]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:52:36 2008'' |
Revision as of 09:52, 21 February 2008
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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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