Spagnol Gaelle, Reiling Calliste, Kieken Fabien, Caplan Steve, Sorgen Paul L
Department of Biochemistry and Molecular Biology and Eppley Cancer Center, University of, Nebraska Medical Center, Omaha, Nebraska 68198.
Biomol NMR Assign. 2014 Oct;8(2):263-267. doi: 10.1007/s12104-013-9497-z. Epub 2013 Jun 11.
The C-terminal Eps15 homology (EH) domain 3 (EHD3) belongs to a eukaryotic family of endocytic regulatory proteins and is involved in the recycling of various receptors from the early endosome to the endocytic recycling compartment or in retrograde transport from the endosomes to the Golgi. EH domains are highly conserved in the EHD family and function as protein-protein interaction units that bind to Asn-Pro-Phe (NPF) motif-containing proteins. The EH domain of EHD1 was the first C-terminal EH domain from the EHD family to be solved by NMR. The differences observed between this domain and proteins with N-terminal EH domains helped describe a mechanism for the differential binding of NPF-containing proteins. Here, structural studies were expanded to include the EHD3 EH domain. While the EHD1 and EHD3 EH domains are highly homologous, they have different protein partners. A comparison of these structures will help determine the selectivity in protein binding between the EHD family members and lead to a better understanding of their unique roles in endocytic regulation.
C 末端 Eps15 同源（EH）结构域 3（EHD3）属于真核细胞内吞调节蛋白家族，参与多种受体从早期内体到内吞循环区室的循环利用，或从内体到高尔基体的逆行转运。EH 结构域在 EHD 家族中高度保守，作为蛋白质 - 蛋白质相互作用单元，与含天冬酰胺 - 脯氨酸 - 苯丙氨酸（NPF）基序的蛋白质结合。EHD1 的 EH 结构域是 EHD 家族中首个通过核磁共振解析的 C 末端 EH 结构域。该结构域与含 N 末端 EH 结构域的蛋白质之间观察到的差异，有助于描述含 NPF 蛋白质差异结合的机制。在此，结构研究扩展至包括 EHD3 的 EH 结构域。虽然 EHD1 和 EHD3 的 EH 结构域高度同源，但它们具有不同的蛋白质伙伴。比较这些结构将有助于确定 EHD 家族成员之间蛋白质结合的选择性，并更好地理解它们在内吞调节中的独特作用。
