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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 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 (mVps28CTD), which is involved in interactions with other ESCRT components. We also compare the predicted secondary structures of mVps28CTD with those of the published X-ray crystal structures of Saccharomyces cerevisiae and Xenopus laevis Vps28CTD. 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biomolecular NMR Assignments Springer Journals

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

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Publisher
Springer Journals
Copyright
Copyright © 2013 by Springer Science+Business Media Dordrecht
Subject
Physics; Biophysics and Biological Physics; Polymer Sciences; Biochemistry, general
ISSN
1874-2718
eISSN
1874-270X
DOI
10.1007/s12104-013-9537-8
pmid
24366722
Publisher site
See Article on Publisher Site

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 (mVps28CTD), which is involved in interactions with other ESCRT components. We also compare the predicted secondary structures of mVps28CTD with those of the published X-ray crystal structures of Saccharomyces cerevisiae and Xenopus laevis Vps28CTD. 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.

Journal

Biomolecular NMR Assignments – Springer Journals

Published: Dec 24, 2013

References

  • Protein-protein interactions of ESCRT complexes in the yeast Saccharomyces cerevisiae
    Bowers, K; Lottridge, J; Helliwell, SB; Goldthwaite, LM; Luzio, JP; Stevens, TH
  • Determination of secondary structure populations in disordered states of proteins using nuclear magnetic resonance chemical shifts
    Camilloni, C; Simone, A; Vranken, WF; Vendruscolo, M
  • DANGLE: A Bayesian inferential method for predicting protein backbone dihedral angles and secondary structure
    Cheung, MS; Maguire, ML; Stevens, TJ; Broadhurst, RW
  • NMRPipe: a multidimensional spectral processing system based on UNIX pipes
    Delaglio, F; Grzesiek, S; Vuister, GW; Zhu, G; Pfeifer, J; Bax, A
  • Structural insight into the ESCRT-I/-II link and its role in MVB trafficking
    Gill, DJ; Teo, H; Sun, J; Perisic, O; Veprintsev, DB; Emr, SD; Williams, RL
  • Multivesicular body morphogenesis
    Hanson, PI; Cashikar, A
  • Integrated structural model and membrane targeting mechanism of the human ESCRT-II complex
    Im, YJ; Hurley, JH
  • NMRViewJ, version 8.2.36
    Johnson, BA
  • The crystal structure of the C-terminal domain of Vps28 reveals a conserved surface required for Vps20 recruitment
    Pineda-Molina, E; Belrhali, H; Piefer, AJ; Akula, I; Bates, P; Weissenhorn, W
  • Biogenesis and function of multivesicular bodies
    Piper, RC; Katzmann, DJ
  • TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    Shen, Y; Delaglio, F; Cornilescu, G; Bax, A
  • ESCRT-I core and ESCRT-II GLUE domain structures reveal role for GLUE in linking to ESCRT-I and membranes
    Teo, H; Gill, DJ; Sun, J; Perisic, O; Veprintsev, DB; Vallis, Y; Emr, SD; Williams, RL