4G2V

Structure complex of LGN binding with FRMPD1

4G2V の概要

• エントリーDOI: 10.2210/pdb4g2v/pdb
• 分子名称: G-protein-signaling modulator 2, peptide from FERM and PDZ domain-containing protein 1, GLYCEROL, ... (6 entities in total)
• 機能のキーワード: tpr repeat, lgn, cell polarity, protein binding
• 由来する生物種: Mus musculus (mouse); 詳細
• 細胞内の位置: Cytoplasm (By similarity): Q8VDU0; Cytoplasm, cytosol: Q5SYB0
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 42673.12

構造登録者

Shang, Y.,Pan, Z.,Wen, W.,Wang, W.,Zhang, M. (登録日: 2012-07-13, 公開日: 2013-01-23, 最終更新日: 2024-03-20)

主引用文献

Pan, Z.,Shang, Y.,Jia, M.,Zhang, L.,Xia, C.,Zhang, M.,Wang, W.,Wen, W.
Structural and biochemical characterization of the interaction between LGN and Frmpd1
J.Mol.Biol., 425:1039-1049, 2013

PubMed Abstract: The tetratricopeptide repeat (TPR) motif-containing protein LGN binds multiple targets and regulates their subcellular localizations and functions during both asymmetric and symmetric cell divisions. Here, we characterized the interaction between LGN-TPR motifs and FERM and PDZ domain containing 1 (Frmpd1) and reported the crystal structure of the complex at 2.4Å resolution. A highly conserved fragment at the center of Frmpd1 of ~20 residues was found to be necessary and sufficient to bind to LGN-TPR. This Frmpd1 fragment forms an extended structure and runs along the concave channel of the TPR superhelix in an antiparallel manner in the complex. Structural comparisons and biochemical studies of LGN/Frmpd1 and other known LGN/target interactions demonstrate that the LGN-TPR motifs are versatile and capable of recognizing multiple targets via diverse binding modes. Nevertheless, a conserved "E/QxEx4-5E/D/Qx1-2K/R" motif in LGN/Pins (partner of inscuteable) TPR binding proteins has been identified.

PubMed: 23318951
DOI: 10.1016/j.jmb.2013.01.003

実験手法

X-RAY DIFFRACTION (2.4 Å)