1xi4: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1xi4.gif|left|200px]] | [[Image:1xi4.gif|left|200px]] | ||
'''Clathrin D6 Coat''' | {{Structure | ||
|PDB= 1xi4 |SIZE=350|CAPTION= <scene name='initialview01'>1xi4</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Clathrin D6 Coat''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1XI4 is a [ | 1XI4 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. The following page contains interesting information on the relation of 1XI4 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=1XI4 OCA]. | ||
==Reference== | ==Reference== | ||
Molecular model for a complete clathrin lattice from electron cryomicroscopy., Fotin A, Cheng Y, Sliz P, Grigorieff N, Harrison SC, Kirchhausen T, Walz T, Nature. 2004 Dec 2;432(7017):573-9. Epub 2004 Oct 24. PMID:[http:// | Molecular model for a complete clathrin lattice from electron cryomicroscopy., Fotin A, Cheng Y, Sliz P, Grigorieff N, Harrison SC, Kirchhausen T, Walz T, Nature. 2004 Dec 2;432(7017):573-9. Epub 2004 Oct 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15502812 15502812] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Clathrin]] | [[Category: Clathrin]] | ||
| Line 25: | Line 34: | ||
[[Category: clathrin]] | [[Category: clathrin]] | ||
''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 15:10:05 2008'' | ||
Revision as of 16:10, 20 March 2008
| |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Clathrin D6 Coat
OverviewOverview
Clathrin-coated vesicles are important vehicles of membrane traffic in cells. We report the structure of a clathrin lattice at subnanometre resolution, obtained from electron cryomicroscopy of coats assembled in vitro. We trace most of the 1,675-residue clathrin heavy chain by fitting known crystal structures of two segments, and homology models of the rest, into the electron microscopy density map. We also define the position of the central helical segment of the light chain. A helical tripod, the carboxy-terminal parts of three heavy chains, projects inward from the vertex of each three-legged clathrin triskelion, linking that vertex to 'ankles' of triskelions centred two vertices away. Analysis of coats with distinct diameters shows an invariant pattern of contacts in the neighbourhood of each vertex, with more variable interactions along the extended parts of the triskelion 'legs'. These invariant local interactions appear to stabilize the lattice, allowing assembly and uncoating to be controlled by events at a few specific sites.
About this StructureAbout this Structure
1XI4 is a Protein complex structure of sequences from Bos taurus. The following page contains interesting information on the relation of 1XI4 with [Clathrin]. Full crystallographic information is available from OCA.
ReferenceReference
Molecular model for a complete clathrin lattice from electron cryomicroscopy., Fotin A, Cheng Y, Sliz P, Grigorieff N, Harrison SC, Kirchhausen T, Walz T, Nature. 2004 Dec 2;432(7017):573-9. Epub 2004 Oct 24. PMID:15502812
Page seeded by OCA on Thu Mar 20 15:10:05 2008