title: Backbone and side-chain NMR assignments for the C-terminal domain of mammalian Vps28.
abstract: Vps28 is one of four cytosolic proteins comprising the endosomal sorting complex required for transport I (ESCRT-I). ESCRT-I is involved in sorting ubiquitinated proteins to multivesicular bodies as well as in mediating budding of retroviruses. Here, we report the backbone and side-chain assignments of the mammalian C-terminal domain of Vps28 (mVps28(CTD)), which is involved in interactions with other ESCRT components. We also compare the predicted secondary structures of mVps28(CTD) with those of the published X-ray crystal structures of Saccharomyces cerevisiae and Xenopus laevis Vps28(CTD). These NMR resonance assignments will facilitate chemical shift mapping and structural determination of mammalian Vps28 interactions with other components of the endosomal sorting machinery that sorts ubiquitinated proteins for lysosomal degradation.
authors.affiliation: Department of Molecular Physiology and Biophysics, University of Iowa, Iowa City, IA, 52242, USA.
authors.forename: Tabitha A
authors.initials: TA
authors.lastname: Peterson
authors.forename: Liping
authors.initials: L
authors.lastname: Yu
authors.forename: Robert C
authors.initials: RC
authors.lastname: Piper
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D056827:Endosomal Sorting Complexes Required for Transport / Q000737:chemistry*; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary
chemical_list: D056827:Endosomal Sorting Complexes Required for Transport; C476409:VPS28 protein, human