EH domain of EHD1 |
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Authors: | Fabien Kieken Marko Jovi? Naava Naslavsky Steve Caplan Paul L Sorgen |
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Institution: | (1) Department of Biochemistry and Molecular Biology and Eppley Cancer Center, University of Nebraska Medical Center, Omaha, NE 68198, USA |
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Abstract: | 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. |
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Keywords: | EHD1 EH domain |
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