7O06
Crystal structure of the N-terminal domain of CEP164(1-109) bound to camelid nanobody 10Z
Summary for 7O06
| Entry DOI | 10.2210/pdb7o06/pdb |
| Descriptor | Camelid nanobody 10Z, Centrosomal protein of 164 kDa, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | centriole, centrosome, basal body, ciliogenesis, cell cycle, structural protein |
| Biological source | Camelidae mixed library More |
| Total number of polymer chains | 4 |
| Total formula weight | 54044.42 |
| Authors | e Silva, I.R.,van Breugel, M. (deposition date: 2021-03-25, release date: 2021-09-08, Last modification date: 2024-01-31) |
| Primary citation | Rosa E Silva, I.,Bino, L.,Johnson, C.M.,Rutherford, T.J.,Neuhaus, D.,Andreeva, A.,Cajanek, L.,van Breugel, M. Molecular mechanisms underlying the role of the centriolar CEP164-TTBK2 complex in ciliopathies. Structure, 30:114-128.e9, 2022 Cited by PubMed Abstract: Cilia formation is essential for human life. One of the earliest events in the ciliogenesis program is the recruitment of tau-tubulin kinase 2 (TTBK2) by the centriole distal appendage component CEP164. Due to the lack of high-resolution structural information on this complex, it is unclear how it is affected in human ciliopathies such as nephronophthisis. Furthermore, it is poorly understood if binding to CEP164 influences TTBK2 activities. Here, we present a detailed biochemical, structural, and functional analysis of the CEP164-TTBK2 complex and demonstrate how it is compromised by two ciliopathic mutations in CEP164. Moreover, we also provide insights into how binding to CEP164 is coordinated with TTBK2 activities. Together, our data deepen our understanding of a crucial step in cilia formation and will inform future studies aimed at restoring CEP164 functionality in a debilitating human ciliopathy. PubMed: 34499853DOI: 10.1016/j.str.2021.08.007 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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