9UHD
Structure of FAM92A BAR domain
Summary for 9UHD
| Entry DOI | 10.2210/pdb9uhd/pdb |
| Descriptor | CBY1-interacting BAR domain-containing protein 1 (2 entities in total) |
| Functional Keywords | protein binding, lipid binding protein |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 25232.56 |
| Authors | |
| Primary citation | Xu, X.,Ren, J.,Li, J. Dimerization of the BAR domain-containing protein FAM92A modulates lipid binding and interaction with CBY1. J.Biol.Chem., 301:110346-110346, 2025 Cited by PubMed Abstract: BAR (Bin/Amphiphysin/Rvs) domain proteins drive membrane remodeling critical for cellular processes like ciliogenesis and organelle morphology. FAM92A (family with sequence similarity 92A), a classical BAR protein, regulates ciliary assembly, mitochondrial ultrastructure, and neuronal membrane dynamics, yet its molecular mechanisms remain elusive. Here, we determined the 2.2 Å crystal structure of the mouse FAM92A BAR domain, revealing an antiparallel, crescent-shaped homodimer. Structure-guided mutagenesis revealed that positively charged clusters on the concave surface are critical for lipid binding and identified residues essential for dimerization. We further demonstrated that FAM92A BAR directly binds the N-terminal region of Chibby1 (CBY1), a ciliary protein, with their respective dimerizations synergistically enhancing affinity. These findings elucidate the structural basis of FAM92A's membrane remodeling and CBY1 interaction, providing a molecular framework for its function in ciliogenesis and suggesting broader implications for FAM92 family proteins. PubMed: 40484380DOI: 10.1016/j.jbc.2025.110346 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.21 Å) |
Structure validation
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