CFAP410 has a bimodular architecture with a conserved surface patch on its N-terminal leucine-rich repeat motif for binding interaction partners.

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Tác giả: Santiago Alonso-Gil, Robbie Crickley, Laryssa V De Liz, Xuan Deng, Gang Dong, Heloisa B Gabriel, Kaiyao Huang, Katharina Korbula, Barbora Mikolaskova, Alexander Stadler, Jack D Sunter, Sue Vaughan, Bojan Žagrović

Ngôn ngữ: eng

Ký hiệu phân loại:

Thông tin xuất bản: Switzerland : Frontiers in cell and developmental biology , 2025

Mô tả vật lý:

Bộ sưu tập: NCBI

ID: 728197

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Cilia and flagella associated protein 410 (CFAP410) is a protein localized at the basal body of cilia/flagella and plays essential roles in ciliogenesis. Multiple single amino acid mutations in CFAP410 have been identified in patients. However, the molecular mechanism for how the mutations cause these disorders remains poorly understood due to a lack of high-resolution structures of the protein. Our studies demonstrate that CFAP410 adopts a bimodular architecture. We have previously reported our structural studies on the C-terminal domain (CTD) of CFAP410 from various organisms. Here we report a 1.0-Å resolution crystal structure of the N-terminal domain (NTD) of

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