2v0x
From Proteopedia
(New page: 200px<br /><applet load="2v0x" size="450" color="white" frame="true" align="right" spinBox="true" caption="2v0x, resolution 2.2Å" /> '''THE DIMERIZATION DOMA...) |
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| - | [[Image:2v0x.gif|left|200px]]<br /><applet load="2v0x" size=" | + | [[Image:2v0x.gif|left|200px]]<br /><applet load="2v0x" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2v0x, resolution 2.2Å" /> | caption="2v0x, resolution 2.2Å" /> | ||
'''THE DIMERIZATION DOMAIN OF LAP2ALPHA'''<br /> | '''THE DIMERIZATION DOMAIN OF LAP2ALPHA'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2V0X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 2V0X is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: phosphorylation]] | [[Category: phosphorylation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:46:18 2008'' |
Revision as of 12:46, 23 January 2008
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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 Wed Jan 23 14:46:18 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 a | Lamina-associated polypeptide | Laminopathy | Nuclear protein | Phosphorylation
