5WRD

Crystal structure of LC3B in complex with FYCO1 LIR

5WRD の概要

• エントリーDOI: 10.2210/pdb5wrd/pdb
• 分子名称: Microtubule-associated proteins 1A/1B light chain 3B, Peptide from FYVE and coiled-coil domain-containing protein 1, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: autophagy, protein binding
• 由来する生物種: Mus musculus (Mouse); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 33826.51

構造登録者

Sakurai, S.,Ohto, U.,Shimizu, T. (登録日: 2016-12-01, 公開日: 2017-03-29, 最終更新日: 2024-11-06)

主引用文献

Sakurai, S.,Tomita, T.,Shimizu, T.,Ohto, U.
The crystal structure of mouse LC3B in complex with the FYCO1 LIR reveals the importance of the flanking region of the LIR motif
Acta Crystallogr F Struct Biol Commun, 73:130-137, 2017

PubMed Abstract: FYVE and coiled-coil domain-containing protein 1 (FYCO1), a multidomain autophagy adaptor protein, mediates microtubule plus-end-directed autophagosome transport by interacting with kinesin motor proteins and with the autophagosomal membrane components microtubule-associated protein 1 light chain 3 (LC3), Rab7 and phosphatidylinositol 3-phosphate (PI3P). To establish the structural basis for the recognition of FYCO1 by LC3, the crystal structure of mouse LC3B in complex with the FYCO1 LC3-interacting region (LIR) motif peptide was determined. Structural analysis showed that the flanking sequences N-terminal and C-terminal to the LIR core sequence of FYCO1, as well as the tetrapeptide core sequence, were specifically recognized by LC3B and contributed to the binding. Moreover, comparisons of related structures revealed a conserved mechanism of FYCO1 recognition by different LC3 isoforms among different species.

PubMed: 28291748
DOI: 10.1107/S2053230X17001911

実験手法

X-RAY DIFFRACTION (1.9 Å)