2L8D

Structure/function of the LBR Tudor domain

2L8D の概要

• エントリーDOI: 10.2210/pdb2l8d/pdb
• NMR情報: BMRB: 17402
• 分子名称: Lamin-B receptor (1 entity in total)
• 機能のキーワード: dna binding protein
• 由来する生物種: Gallus gallus (bantam,chickens)
• 細胞内の位置: Nucleus inner membrane; Multi-pass membrane protein: P23913
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7490.40

構造登録者

Liokatis, S.,Edlich, C.,Soupsana, K.,Giannios, I.,Sattler, M.,Georgatos, S.D.,Politou, A.S. (登録日: 2011-01-10, 公開日: 2011-11-09, 最終更新日: 2024-05-15)

主引用文献

Liokatis, S.,Edlich, C.,Soupsana, K.,Giannios, I.,Panagiotidou, P.,Tripsianes, K.,Sattler, M.,Georgatos, S.D.,Politou, A.S.
Solution structure and molecular interactions of lamin B receptor tudor domain.
J.Biol.Chem., 287:1032-1042, 2012

PubMed Abstract: Lamin B receptor (LBR) is a polytopic protein of the nuclear envelope thought to connect the inner nuclear membrane with the underlying nuclear lamina and peripheral heterochromatin. To better understand the function of this protein, we have examined in detail its nucleoplasmic region, which is predicted to harbor a Tudor domain (LBR-TD). Structural analysis by multidimensional NMR spectroscopy establishes that LBR-TD indeed adopts a classical β-barrel Tudor fold in solution, which, however, features an incomplete aromatic cage. Removal of LBR-TD renders LBR more mobile at the plane of the nuclear envelope, but the isolated module does not bind to nuclear lamins, heterochromatin proteins (MeCP2), and nucleosomes, nor does it associate with methylated Arg/Lys residues through its aromatic cage. Instead, LBR-TD exhibits tight and stoichiometric binding to the "histone-fold" region of unassembled, free histone H3, suggesting an interesting role in histone assembly. Consistent with such a role, robust binding to native nucleosomes is observed when LBR-TD is extended toward its carboxyl terminus, to include an area rich in Ser-Arg residues. The Ser-Arg region, alone or in combination with LBR-TD, binds both unassembled and assembled H3/H4 histones, suggesting that the TD/RS interface may operate as a "histone chaperone-like platform."

PubMed: 22052904
DOI: 10.1074/jbc.M111.281303

実験手法

SOLUTION NMR