6wud

Human Calcium and Integrin Binding Protein 3 Bound to TMC1 Residues 303-347

spinqualitylabelsall models 6wud, resolution 1.84Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6wud is a 2 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.84Å Ligands: MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CIB3_HUMAN Publication Abstract from PubMed CIB2 is a Ca(2+)- and Mg(2+)-binding protein essential for mechanoelectrical transduction (MET) by cochlear hair cells, but not by vestibular hair cells that co-express CIB2 and CIB3. Here, we show that in cochlear hair cells, CIB3 can functionally substitute for CIB2. Using X-ray crystallography, we demonstrate that CIB2 and CIB3 are structurally similar to KChIP proteins, auxiliary subunits of voltage-gated Kv4 channels. CIB2 and CIB3 bind to TMC1/2 through a domain in TMC1/2 flanked by transmembrane domains 2 and 3. The co-crystal structure of the CIB-binding domain in TMC1 with CIB3 reveals that interactions are mediated through a conserved CIB hydrophobic groove, similar to KChIP1 binding of Kv4. Functional studies in mice show that CIB2 regulates TMC1/2 localization and function in hair cells, processes that are affected by deafness-causing CIB2 mutations. We conclude that CIB2 and CIB3 are MET channel auxiliary subunits with striking similarity to Kv4 channel auxiliary subunits. CIB2 and CIB3 are auxiliary subunits of the mechanotransduction channel of hair cells.,Liang X, Qiu X, Dionne G, Cunningham CL, Pucak ML, Peng G, Kim YH, Lauer A, Shapiro L, Muller U Neuron. 2021 Jul 7;109(13):2131-2149.e15. doi: 10.1016/j.neuron.2021.05.007. Epub, 2021 Jun 5. PMID:34089643 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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