4xhz | pdb_00004xhz

Crystal Structure of Human Protocadherin-15 EC8-10

spinqualitylabelsall models 4xhz, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4xhz is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.803Å Ligands: CA, CL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease PCD15_HUMAN Usher syndrome type 1;Autosomal recessive non-syndromic sensorineural deafness type DFNB. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. Function PCD15_HUMAN Calcium-dependent cell-adhesion protein. Essential for maintenance of normal retinal and cochlear function. Publication Abstract from PubMed Tip link filaments convey force and gate inner-ear hair-cell transduction channels to mediate perception of sound and head movements. Cadherin-23 and protocadherin-15 form tip links through a calcium-dependent interaction of their extracellular domains made of multiple extracellular cadherin (EC) repeats. These repeats are structurally similar, but not identical in sequence, often featuring linkers with conserved calcium-binding sites that confer mechanical strength to them. Here we present the X-ray crystal structures of human protocadherin-15 EC8-EC10 and mouse EC9-EC10, which show an EC8-9 canonical-like calcium-binding linker, and an EC9-10 calcium-free linker that alters the linear arrangement of EC repeats. Molecular dynamics simulations and small-angle X-ray scattering experiments support this non-linear conformation. Simulations also suggest that unbending of EC9-10 confers some elasticity to otherwise rigid tip links. The new structure provides a first view of protocadherin-15's non-canonical EC linkers and suggests how they may function in inner-ear mechanotransduction, with implications for other cadherins. An elastic element in the protocadherin-15 tip link of the inner ear.,Araya-Secchi R, Neel BL, Sotomayor M Nat Commun. 2016 Nov 18;7:13458. doi: 10.1038/ncomms13458. PMID:27857071 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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