Kieken Fabien, Jović Marko, Naslavsky Naava, Caplan Steve, Sorgen Paul L
Department of Biochemistry and Molecular Biology and Eppley Cancer Center, University of Nebraska Medical Center, Omaha, NE 68198, USA.
J Biomol NMR. 2007 Dec;39(4):323-9. doi: 10.1007/s10858-007-9196-0. Epub 2007 Sep 26.
EHD1 is a member of the mammalian C-terminal Eps15 homology domain (EH) containing protein family, and regulates the recycling of various receptors from the endocytic recycling compartment to the plasma membrane. The EH domain of EHD1 binds to proteins containing either an Asn-Pro-Phe or Asp-Pro-Phe motif, and plays an important role in the subcellular localization and function of EHD1. Thus far, the structures of five N-terminal EH domains from other proteins have been solved, but to date, the structure of the EH domains from the four C-terminal EHD family paralogs remains unknown. In this study, we have assigned the 133 C-terminal residues of EHD1, which includes the EH domain, and solved its solution structure. While the overall structure resembles that of the second of the three N-terminal Eps15 EH domains, potentially significant differences in surface charge and the structure of the tripeptide-binding pocket are discussed.
EHD1是哺乳动物含C端Eps15同源结构域(EH)蛋白家族的成员,可调节多种受体从胞吞循环区室到质膜的循环利用。EHD1的EH结构域与含有天冬酰胺-脯氨酸-苯丙氨酸或天冬氨酸-脯氨酸-苯丙氨酸基序的蛋白质结合,并在EHD1的亚细胞定位和功能中发挥重要作用。迄今为止,已解析了来自其他蛋白质的五个N端EH结构域的结构,但到目前为止,四个C端EHD家族旁系同源物的EH结构域的结构仍然未知。在本研究中,我们确定了EHD1的133个C端残基,其中包括EH结构域,并解析了其溶液结构。虽然整体结构类似于三个N端Eps15 EH结构域中的第二个,但讨论了表面电荷和三肽结合口袋结构的潜在显著差异。