2V0X

The dimerization domain of LAP2alpha

Summary for 2V0X

• Entry DOI: 10.2210/pdb2v0x/pdb
• Descriptor: LAMINA-ASSOCIATED POLYPEPTIDE 2 ISOFORMS ALPHA/ZETA (2 entities in total)
• Functional Keywords: alternative splicing, lamina-associated polypeptide, nuclear protein, phosphorylation, chromosomal protein, lamin a, coiled coil, dna-binding, laminopathy, cell cycle
• Biological source: MUS MUSCULUS (MOUSE)
• Total number of polymer chains: 2
• Total formula weight: 51089.07

Authors

Bradley, C.M.,Jones, S.,Huang, Y.,Suzuki, Y.,Kvaratskhelia, M.,Hickman, A.B.,Craigie, R.,Dyda, F. (deposition date: 2007-05-20, release date: 2007-06-26, Last modification date: 2024-10-16)

Primary citation

Bradley, C.M.,Jones, S.,Huang, Y.,Suzuki, Y.,Kvaratskhelia, M.,Hickman, A.B.,Craigie, R.,Dyda, F.
Structural Basis for Dimerization of Lap2Alpha, a Component of the Nuclear Lamina.
Structure, 15:643-, 2007

PubMed Abstract: 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.

PubMed: 17562312
DOI: 10.1016/J.STR.2007.04.007

Experimental method

X-RAY DIFFRACTION (2.2 Å)