2V0X

The dimerization domain of LAP2alpha

2V0X の概要

• エントリーDOI: 10.2210/pdb2v0x/pdb
• 分子名称: LAMINA-ASSOCIATED POLYPEPTIDE 2 ISOFORMS ALPHA/ZETA (2 entities in total)
• 機能のキーワード: alternative splicing, lamina-associated polypeptide, nuclear protein, phosphorylation, chromosomal protein, lamin a, coiled coil, dna-binding, laminopathy, cell cycle
• 由来する生物種: MUS MUSCULUS (MOUSE)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 51089.07

構造登録者

Bradley, C.M.,Jones, S.,Huang, Y.,Suzuki, Y.,Kvaratskhelia, M.,Hickman, A.B.,Craigie, R.,Dyda, F. (登録日: 2007-05-20, 公開日: 2007-06-26, 最終更新日: 2024-10-16)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.2 Å)