2LQR

NMR structure of Ig3 domain of palladin

2LQR の概要

• エントリーDOI: 10.2210/pdb2lqr/pdb
• NMR情報: BMRB: 15512
• 分子名称: Palladin (1 entity in total)
• 機能のキーワード: actin binding protein, immunoglubulin, protein binding
• 由来する生物種: Mus musculus (mouse)
• 細胞内の位置: Cytoplasm, cytoskeleton: Q9ET54
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11991.61

構造登録者

Beck, M.R.,Dixon IV, R.D.S.,Otey, C.A.,Campbell, S.L.,Murphy, G.S. (登録日: 2012-03-13, 公開日: 2013-01-23, 最終更新日: 2024-05-01)

主引用文献

Beck, M.R.,Dixon, R.D.,Goicoechea, S.M.,Murphy, G.S.,Brungardt, J.G.,Beam, M.T.,Srinath, P.,Patel, J.,Mohiuddin, J.,Otey, C.A.,Campbell, S.L.
Structure and Function of Palladin's Actin Binding Domain.
J.Mol.Biol., 425:3325-3337, 2013

PubMed Abstract: Here, we report the NMR structure of the actin-binding domain contained in the cell adhesion protein palladin. Previously, we demonstrated that one of the immunoglobulin domains of palladin (Ig3) is both necessary and sufficient for direct filamentous actin binding in vitro. In this study, we identify two basic patches on opposite faces of Ig3 that are critical for actin binding and cross-linking. Sedimentation equilibrium assays indicate that the Ig3 domain of palladin does not self-associate. These combined data are consistent with an actin cross-linking mechanism that involves concurrent attachment of two actin filaments by a single palladin molecule by an electrostatic mechanism. Palladin mutations that disrupt actin binding show altered cellular distributions and morphology of actin in cells, revealing a functional requirement for the interaction between palladin and actin in vivo.

PubMed: 23806659
DOI: 10.1016/j.jmb.2013.06.016

実験手法

SOLUTION NMR