4WNE

Crystal structure of the TPR domain of LGN in complex with Frmpd4/Preso1 at 2.0 Angstrom resolution

4WNE の概要

• エントリーDOI: 10.2210/pdb4wne/pdb
• 関連するPDBエントリー: 3SF4 4WND 4WNF 4WNG
• 分子名称: G-protein-signaling modulator 2, Peptide from FERM and PDZ domain-containing protein 4 (3 entities in total)
• 機能のキーワード: tetratricopeptide repeat, tpr, cell polarity, cytoplasm and cell cortex, signaling protein-protein binding complex, signaling protein/protein binding
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47979.67

構造登録者

Takayanagi, H.,Yuzawa, S.,Sumimoto, H. (登録日: 2014-10-11, 公開日: 2015-09-16, 最終更新日: 2023-11-08)

主引用文献

Takayanagi, H.,Yuzawa, S.,Sumimoto, H.
Structural basis for the recognition of the scaffold protein Frmpd4/Preso1 by the TPR domain of the adaptor protein LGN
Acta Crystallogr.,Sect.F, 71:175-183, 2015

PubMed Abstract: The adaptor protein LGN interacts via the N-terminal domain comprising eight tetratricopeptide-repeat (TPR) motifs with its partner proteins mInsc, NuMA, Frmpd1 and Frmpd4 in a mutually exclusive manner. Here, the crystal structure of the LGN TPR domain in complex with human Frmpd4 is described at 1.5 Å resolution. In the complex, the LGN-binding region of Frmpd4 (amino-acid residues 990-1011) adopts an extended structure that runs antiparallel to LGN along the concave surface of the superhelix formed by the TPR motifs. Comparison with the previously determined structures of the LGN-Frmpd1, LGN-mInsc and LGN-NuMA complexes reveals that these partner proteins interact with LGN TPR1-6 via a common core binding region with consensus sequence (E/Q)XEX4-5(E/D/Q)X1-2(K/R)X0-1(V/I). In contrast to Frmpd1, Frmpd4 makes additional contacts with LGN via regions N- and C-terminal to the core sequence. The N-terminal extension is replaced by a specific α-helix in mInsc, which drastically increases the direct contacts with LGN TPR7/8, consistent with the higher affinity of mInsc for LGN. A crystal structure of Frmpd4-bound LGN in an oxidized form is also reported, although oxidation does not appear to strongly affect the interaction with Frmpd4.

PubMed: 25664792
DOI: 10.1107/S2053230X14028143

実験手法

X-RAY DIFFRACTION (2 Å)