2v0x
From Proteopedia
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| - | [[Image:2v0x.gif|left|200px]] | + | [[Image:2v0x.gif|left|200px]] |
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| - | '''THE DIMERIZATION DOMAIN OF LAP2ALPHA''' | + | {{Structure |
| + | |PDB= 2v0x |SIZE=350|CAPTION= <scene name='initialview01'>2v0x</scene>, resolution 2.2Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''THE DIMERIZATION DOMAIN OF LAP2ALPHA''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2V0X is a [ | + | 2V0X is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V0X OCA]. |
==Reference== | ==Reference== | ||
| - | Structural basis for dimerization of LAP2alpha, a component of the nuclear lamina., Bradley CM, Jones S, Huang Y, Suzuki Y, Kvaratskhelia M, Hickman AB, Craigie R, Dyda F, Structure. 2007 Jun;15(6):643-53. PMID:[http:// | + | Structural basis for dimerization of LAP2alpha, a component of the nuclear lamina., Bradley CM, Jones S, Huang Y, Suzuki Y, Kvaratskhelia M, Hickman AB, Craigie R, Dyda F, Structure. 2007 Jun;15(6):643-53. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17562312 17562312] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: coiled coil]] | [[Category: coiled coil]] | ||
[[Category: dna-binding]] | [[Category: dna-binding]] | ||
| - | [[Category: lamin | + | [[Category: lamin some]] |
[[Category: lamina-associated polypeptide]] | [[Category: lamina-associated polypeptide]] | ||
[[Category: laminopathy]] | [[Category: laminopathy]] | ||
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[[Category: phosphorylation]] | [[Category: phosphorylation]] | ||
| - | ''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 18:42:06 2008'' |
Revision as of 16:42, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE DIMERIZATION DOMAIN OF LAP2ALPHA
Overview
Lamina-associated polypeptides (LAPs) are important components of the nuclear lamina, the dense network of filaments that supports the nuclear envelope and also extends into the nucleoplasm. The main protein constituents of the nuclear lamina are the constitutively expressed B-type lamins and the developmentally regulated A- and C-type lamins. LAP2alpha is the only non-membrane-associated member of the LAP family. It preferentially binds lamin A/C, has been implicated in cell-cycle regulation and chromatin organization, and has also been found to be a component of retroviral preintegration complexes. As an approach to understanding the role of LAP2alpha in cellular pathways, we have determined the crystal structure of the C-terminal domain of LAP2alpha, residues 459-693. The C-terminal domain is dimeric and possesses an extensive four-stranded, antiparallel coiled coil. The surface involved in binding lamin A/C is proposed based on results from alanine-scanning mutagenesis and a solid-phase overlay binding assay.
About this Structure
2V0X is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural basis for dimerization of LAP2alpha, a component of the nuclear lamina., Bradley CM, Jones S, Huang Y, Suzuki Y, Kvaratskhelia M, Hickman AB, Craigie R, Dyda F, Structure. 2007 Jun;15(6):643-53. PMID:17562312
Page seeded by OCA on Thu Mar 20 18:42:06 2008
Categories: Mus musculus | Single protein | Bradley, C M. | Craigie, R. | Dyda, F. | Hickman, A B. | Huang, Y. | Jones, S. | Kvaratskhelia, M. | Suzuki, Y. | Alternative splicing | Cell cycle | Chromosomal protein | Coiled coil | Dna-binding | Lamin some | Lamina-associated polypeptide | Laminopathy | Nuclear protein | Phosphorylation
