7EL6

Structure of SMCR8 bound FEM1B

7EL6 の概要

• エントリーDOI: 10.2210/pdb7el6/pdb
• 分子名称: Protein fem-1 homolog B,Guanine nucleotide exchange protein SMCR8 (1 entity in total)
• 機能のキーワード: ubiquitination e3 ligase, peptide binding protein
• 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: 78603.55

構造登録者

Zhao, S.,Xu, C. (登録日: 2021-04-08, 公開日: 2021-05-12, 最終更新日: 2023-11-29)

主引用文献

Zhao, S.,Ru, W.,Chen, X.,Liao, S.,Zhu, Z.,Zhang, J.,Xu, C.
Structural insights into SMCR8 C-degron recognition by FEM1B.
Biochem.Biophys.Res.Commun., 557:236-239, 2021

PubMed Abstract: C-degrons play critical roles in targeting the receptor proteins of Cullin-RING E3 ligase complexes to initiate protein degradation. FEM1 proteins, including FEM1A, FEM1B, and FEM1C, act as the receptors to specifically recognize Arg/C-degrons to enable CRL2-mediated protein turnover. Very few substrates have been identified for FEM1B, except CDK5R1. We found that CRL2 also recognizes the C-degron of an SMCR8 isoform, and uncovered the recognition of SMCR8 by FEM1B through presenting the structure of FEM1B bound to SMCR8. Our work provides insights into the role of CRL2 in regulating the lifetime of SMCR8, a critical autophagy regulator.

PubMed: 33892462
DOI: 10.1016/j.bbrc.2021.04.046

実験手法

X-RAY DIFFRACTION (2.802 Å)