6y9p

Crystal structure of Whirlin PDZ3_C-ter in complex with Harmonin a1 C-terminal PDZ binding motif peptide

spinqualitylabelsall models 6y9p, resolution 3.17Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6y9p is a 12 chain structure with sequence from Mus musculus and Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.169Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease WHRN_MOUSE Defects in Whrn are the cause of the phenotype whirler (wi). Mutants are characterized by deafness due to malformation of the cochlear inner and outer hair cells and by circling behavior. Stereocilia are shorter and wider than in wild-type animals and there is a decrease in the number of actin filaments in inner and outer hair cells. The number of outer hair cell stereocilia is reduced with increased spacing between them. Function WHRN_MOUSE Necessary for elongation and maintenance of inner and outer hair cell stereocilia in the organ of Corti in the inner ear. Publication Abstract from PubMed Hearing is a mechanical and neurochemical process, which occurs in the hair cells of inner ear that converts the sound vibrations into electrical signals transmitted to the brain. The multi-PDZ scaffolding protein whirlin plays a critical role in the formation and function of stereocilia exposed at the surface of hair cells. In this article, we reported seven stereociliary proteins that encode PDZ binding motifs (PBM) and interact with whirlin PDZ3, where four of them are first reported. We solved the atomic resolution structures of complexes between whirlin PDZ3 and the PBMs of myosin 15a, CASK, harmonin a1 and taperin. Interestingly, the PBM of CASK and taperin are rare non-canonical PBM, that are not localized at the extreme C-terminus. This large capacity to accommodate various partners could be related to the distinct functions of whirlin at different stages of the hair cell development. Deciphering the Unexpected Binding Capacity of the Third PDZ Domain of Whirlin to Various Cochlear Hair Cell Partners.,Zhu Y, Delhommel F, Cordier F, LUchow S, Mechaly A, Colcombet-Cazenave B, Girault V, Pepermans E, Bahloul A, Gautier C, Brule S, Raynal B, Hoos S, Haouz A, Caillet-Saguy C, Ivarsson Y, Wolff N J Mol Biol. 2020 Sep 21. pii: S0022-2836(20)30554-4. doi:, 10.1016/j.jmb.2020.09.012. PMID:32971111 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA