7EAA

crystal structure of NDP52 SKICH domain in complex with RB1CC1 coiled-coil domain

Summary for 7EAA

• Entry DOI: 10.2210/pdb7eaa/pdb
• Descriptor: RB1-inducible coiled-coil protein 1, Calcium-binding and coiled-coil domain-containing protein 2 (3 entities in total)
• Functional Keywords: ndp52 skich, complex, rb1cc1 coiled-coil, protein binding
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 4
• Total formula weight: 59068.20

Authors

Fu, T.,Pan, L. (deposition date: 2021-03-06, release date: 2021-12-22, Last modification date: 2023-11-29)

Primary citation

Fu, T.,Zhang, M.,Zhou, Z.,Wu, P.,Peng, C.,Wang, Y.,Gong, X.,Li, Y.,Wang, Y.,Xu, X.,Li, M.,Shen, L.,Pan, L.
Structural and biochemical advances on the recruitment of the autophagy-initiating ULK and TBK1 complexes by autophagy receptor NDP52.
Sci Adv, 7:-, 2021

PubMed Abstract: The recruitment of Unc-51-like kinase and TANK-binding kinase 1 complexes is essential for Nuclear dot protein 52-mediated selective autophagy and relies on the specific association of NDP52, RB1-inducible coiled-coil protein 1, and Nak-associated protein 1 (5-azacytidine-induced protein 2, AZI2). However, the underlying molecular mechanism remains elusive. Here, we find that except for the NDP52 SKIP carboxyl homology (SKICH)/RB1CC1 coiled-coil interaction, the LC3-interacting region of NDP52 can directly interact with the RB1CC1 Claw domain, as that of NAP1 FIP200-binding region (FIR). The determined crystal structures of NDP52 SKICH/RB1CC1 complex, NAP1 FIR/RB1CC1 complex, and the related NAP1 FIR/Gamma-aminobutyric acid receptor-associated protein complex not only elucidate the molecular bases underpinning the interactions of RB1CC1 with NDP52 and NAP1 but also reveal that RB1CC1 Claw and Autophagy-related protein 8 family proteins are competitive in binding to NAP1 and NDP52. Overall, our findings provide mechanistic insights into the interactions of NDP52, NAP1 with RB1CC1 and ATG8 family proteins.

PubMed: 34389544
DOI: 10.1126/sciadv.abi6582

Experimental method

X-RAY DIFFRACTION (2.6 Å)