Logo image
Backbone and side-chain NMR assignments for the C-terminal domain of mammalian Vps28
Journal article   Peer reviewed

Backbone and side-chain NMR assignments for the C-terminal domain of mammalian Vps28

Tabitha A. Peterson, Liping Yu and Robert C. Piper
Biomolecular NMR assignments, Vol.9(1), pp.21-24
04/01/2015
DOI: 10.1007/s12104-013-9537-8
PMCID: PMC4470380
PMID: 24366722

View Online

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.
Biophysics Life Sciences & Biomedicine Science & Technology Spectroscopy Technology

Details

Metrics

Logo image