title: Chemical shift assignments of the C-terminal Eps15 homology domain-3 EH domain.
abstract: 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.
authors.affiliation: Department of Biochemistry and Molecular Biology and Eppley Cancer Center, University of, Nebraska Medical Center, Omaha, Nebraska 68198.
authors.forename: Gaelle
authors.initials: G
authors.lastname: Spagnol
authors.affiliation: Department of Biochemistry and Molecular Biology and Eppley Cancer Center, University of, Nebraska Medical Center, Omaha, Nebraska 68198.
authors.forename: Calliste
authors.initials: C
authors.lastname: Reiling
authors.affiliation: Department of Biochemistry and Molecular Biology and Eppley Cancer Center, University of, Nebraska Medical Center, Omaha, Nebraska 68198.
authors.forename: Fabien
authors.initials: F
authors.lastname: Kieken
authors.affiliation: Department of Biochemistry and Molecular Biology and Eppley Cancer Center, University of, Nebraska Medical Center, Omaha, Nebraska 68198.
authors.forename: Steve
authors.initials: S
authors.lastname: Caplan
authors.affiliation: Department of Biochemistry and Molecular Biology and Eppley Cancer Center, University of, Nebraska Medical Center, Omaha, Nebraska 68198.
authors.forename: Paul L
authors.initials: PL
authors.lastname: Sorgen
mesh_terms: D000595:Amino Acid Sequence; D002352:Carrier Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary
chemical_list: D002352:Carrier Proteins