Hudson Jonathan D, Tamilselvan Elakkiya, Sotomayor Marcos, Cooper Sharon R
Department of Science and Mathematics, Cedarville University, 251 N. Main Street, Cedarville, OH 45314, USA.
Department of Chemistry and Biochemistry, The Ohio State University, 484 W. 12th Avenue, Columbus, OH 43210, USA; Biophysics Graduate Program, The Ohio State University, 484 W. 12th Avenue, Columbus, OH 43210, USA.
Structure. 2021 Oct 7;29(10):1128-1143.e4. doi: 10.1016/j.str.2021.07.006. Epub 2021 Sep 13.
Cadherin superfamily members play a critical role in differential adhesion during neurodevelopment, and their disruption has been linked to several neurodevelopmental disorders. Mutations in protocadherin-19 (PCDH19), a member of the δ-protocadherin subfamily of cadherins, cause a unique form of epilepsy called PCDH19 clustering epilepsy. While PCDH19 and other non-clustered δ-protocadherins form multimers with other members of the cadherin superfamily to alter adhesiveness, the specific protein surfaces responsible for these interactions are unknown. Only portions of the PCDH19 extracellular domain structure had been solved previously. Here, we present a structure of the missing segment from zebrafish Protocadherin-19 (Pcdh19) and create a complete ectodomain model. This model shows the structural environment for 97% of disease-causing missense mutations and reveals two potential surfaces for intermolecular interactions that could modify Pcdh19's adhesive strength and specificity.
钙黏蛋白超家族成员在神经发育过程中的差异黏附中发挥关键作用,其功能破坏与多种神经发育障碍有关。原钙黏蛋白-19(PCDH19)是钙黏蛋白δ-原钙黏蛋白亚家族的成员,其突变会导致一种名为PCDH19聚集性癫痫的独特癫痫形式。虽然PCDH19和其他非聚集性δ-原钙黏蛋白与钙黏蛋白超家族的其他成员形成多聚体以改变黏附性,但负责这些相互作用的特定蛋白质表面尚不清楚。此前仅解析了PCDH19细胞外结构域的部分结构。在此,我们展示了斑马鱼原钙黏蛋白-19(Pcdh19)缺失片段的结构,并创建了一个完整的胞外域模型。该模型展示了97%致病错义突变的结构环境,并揭示了两个可能用于分子间相互作用的潜在表面,这些相互作用可能会改变Pcdh19的黏附强度和特异性。