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

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

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

Biomol NMR Assign. 2013 Dec 24;

Authors: Peterson TA, Yu L, Piper RC

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.


PMID: 24366722 [PubMed - as supplied by publisher]



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