7YFU

Structure of Rpgrip1l CC2

Summary for 7YFU

• Entry DOI: 10.2210/pdb7yfu/pdb
• Descriptor: Protein fantom (2 entities in total)
• Functional Keywords: structural protein, protein binding
• Biological source: Mus musculus (house mouse)
• Total number of polymer chains: 2
• Total formula weight: 10505.82

Authors

He, R.,Chen, G.,Li, Z.,Li, J. (deposition date: 2022-07-09, release date: 2023-05-17, Last modification date: 2024-05-29)

Primary citation

He, R.,Chen, G.,Li, Z.,Li, J.
Structure of the N-terminal coiled-coil domains of the ciliary protein Rpgrip1l.
Iscience, 26:106249-106249, 2023

PubMed Abstract: Rpgrip1l is one of the key ciliary proteins located at the transition zone of the primary cilium, an important organelle for cells to sense the outer environment. Mutations in the gene are associated with various ciliopathies. Here, we focused on the N-terminal coiled-coil of Rpgrip1l. By comprehensive biochemical and structural characterizations, we demonstrated that the two predicted coiled-coil regions (CC12) located at Rpgrip1l N-terminus each can form a stable parallel dimer. We further showed that overexpression of Rpgrip1l CC12 in NIH/3T3 cells significantly shortened the length of primary cilia, and this effect depended on the dimer formation. In addition, we found that CC12 of the homolog protein Rpgrip1 in mouse and human were significantly different from Rpgrip1l. Finally, we confirmed that some disease-related mutations can alter the dimeric states of CC12 of Rpgrip1l or Rpgrip1, which might explain the pathogenic mechanisms.

PubMed: 36915689
DOI: 10.1016/j.isci.2023.106249

Experimental method

X-RAY DIFFRACTION (1.5 Å)