5F3X

Crystal structure of Harmonin NPDZ1 in complex with ANKS4B SAM-PBM

Summary for 5F3X

• Entry DOI: 10.2210/pdb5f3x/pdb
• Related: 5F3Y
• Descriptor: Harmonin, Ankyrin repeat and SAM domain-containing protein 4B, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: complex, structural protein, protein binding, structural protein-protein binding complex, structural protein/protein binding
• Biological source: Homo sapiens (Human); More
• Cellular location: Cytoplasm, cytosol: Q9Y6N9
• Total number of polymer chains: 4
• Total formula weight: 62935.06

Authors

Li, J.,He, Y.,Lu, Q.,Zhang, M. (deposition date: 2015-12-03, release date: 2016-03-16, Last modification date: 2023-11-08)

Primary citation

Li, J.,He, Y.,Lu, Q.,Zhang, M.
Mechanistic Basis of Organization of the Harmonin/USH1C-Mediated Brush Border Microvilli Tip-Link Complex
Dev.Cell, 36:179-189, 2016

PubMed Abstract: Brush border microvilli are actin-based protrusions lining the apical surface of epithelial cells in intestines and proximal tubules of kidneys. While brush border microvilli resemble the relatively well-characterized stereocilia of hair cells, the mechanistic basis of tip-link complex organization in microvilli is poorly understood. Here, we have biochemically and structurally characterized the following pairs of interactions: protocadherin 24 and Harmonin (also known as USH1C or AIE-75), Harmonin and myosin VIIb (MYO7B), Harmonin and ANKS4B, and ANKS4B and MYO7B. We show that Harmonin, ANKS4B, and MYO7B form a stable ternary complex for anchoring microvilli tip-link cadherins. Despite having only Harmonin in common, the microvilli and the stereocilia tip-link complexes are formed via strikingly similar interaction modes. These results not only provide insight into the mechanistic bases of brush border microvilli formation and maintenance but may also be valuable for understanding some gut and/or kidney diseases caused by perturbations of brush border microvilli structures.

PubMed: 26812017
DOI: 10.1016/j.devcel.2015.12.020

Experimental method

X-RAY DIFFRACTION (2.649 Å)