Related ArticlesNMR studies on the interactions between yeast Vta1 and Did2 during the multivesicular bodies sorting pathway.
Sci Rep. 2016 12 07;6:38710
Authors: Shen J, Yang Z, Wang J, Zhao B, Lan W, Wang C, Zhang X, Wild CJ, Liu M, Xu Z, Cao C
Abstract
As an AAA-ATPase, Vps4 is important for function of multivesicular bodies (MVB) sorting pathway, which involves in cellular phenomena ranging from receptor down-regulation to viral budding to cytokinesis. The activity of Vps4 is stimulated by the interactions between Vta1 N-terminus (named as Vta1NTD) and Did2 fragment (176-204 aa) (termed as Did2176-204) or Vps60 (128-186 aa) (termed as Vps60128-186). The structural basis of how Vta1NTD binds to Did2176-204 is still unclear. To address this, in this report, the structure of Did2176-204 in complex with Vta1NTD was determined by NMR techniques, demonstrating that Did2176-204 interacts with Vta1NTD through its helix ?6' extending over the 2nd and the 3rd ?-helices of Vta1NTD microtubule interacting and transport 1 (MIT1) domain. The residues within Did2176-204 helix ?6' in the interface make up of an amino acid sequence as E192'xxL195'xxR198'L199'xxL202'R203', identical to type 1 MIT-interacting motif (MIM1) (D/E)xxLxxRLxxL(K/R) of CHMP1A180-196 observed in Vps4-CHMP1A complex structure, indicating that Did2 binds to Vta1NTD through canonical MIM1 interactions. Moreover, the Did2 binding does not result in Vta1NTD significant conformational changes, revealing that Did2, similar to Vps60, enhances Vta1 stimulation of Vps4 ATPase activity in an indirect manner.
Precursor–Receptor Interactions in the TwinArginine Protein Transport Pathway Probed with a New Receptor ComplexPreparation
Precursor–Receptor Interactions in the TwinArginine Protein Transport Pathway Probed with a New Receptor ComplexPreparation
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00026/20180226/images/medium/bi-2018-00026r_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00026
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[NMR paper] Exploring the Protein Folding Pathway with High-Pressure NMR: Steady-State and Kinetics Studies.
Exploring the Protein Folding Pathway with High-Pressure NMR: Steady-State and Kinetics Studies.
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Subcell Biochem. 2015;72:261-278
Authors: Roche J, Dellarole M, Royer CA, Roumestand C
Abstract
Defining the physical-chemical determinants of protein folding and stability, under normal and pathological conditions has constituted a major subfield in biophysical chemistry for over 50 years. Although a great deal of...
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[NMR paper] Electrostatic interactions in the binding pathway of a transient protein complex studied by NMR and isothermal titration calorimetry.
Electrostatic interactions in the binding pathway of a transient protein complex studied by NMR and isothermal titration calorimetry.
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J Biol Chem. 2014 Aug 13;
Authors: Meneses E, Mittermaier A
Abstract
Much of our knowledge of protein binding pathways is derived from extremely stable complexes that interact very tightly, with lifetimes of hours to days. Much less is known about...
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[NMR paper] Practical applications of hydrostatic pressure to refold proteins from inclusion bodies for NMR structural studies.
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Protein Eng Des Sel. 2013 Mar 22;
Authors: Ogura K, Kobashigawa Y, Saio T, Kumeta H, Torikai S, Inagaki F
Abstract
Recently, the hydrostatic pressure refolding method was reported as a practical tool for solubilizing and refolding proteins from inclusion bodies; however, there have been...
Nonnative Interactions in the FF Domain Folding Pathway from an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study
Nonnative Interactions in the FF Domain Folding Pathway from an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study
Dmitry M. Korzhnev, Robert M. Vernon, Tomasz L. Religa, Alexandar L. Hansen, David Baker, Alan R. Fersht and Lewis E. Kay
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja203686t/aop/images/medium/ja-2011-03686t_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja203686t
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Non-Native Interactions in the FF Domain Folding Pathway From an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study.
Non-Native Interactions in the FF Domain Folding Pathway From an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study.
Non-Native Interactions in the FF Domain Folding Pathway From an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study.
J Am Chem Soc. 2011 Jun 6;
Authors: Korzhnev DM, Vernon RM, Religa TL, Hansen AL, Baker D, Fersht AR, Kay LE
Several all-helical single-domain proteins have been shown to fold rapidly (us timescale) to a compact...
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[NMR paper] NMR studies of CCK-8/CCK1 complex support membrane-associated pathway for ligand-rece
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Can J Physiol Pharmacol. 2002 May;80(5):383-7
Authors: Giragossian C, Pellegrini M, Mierke DF
The interaction of peptide ligands with their associated G-protein-coupled receptors has been examined by a number of different experimental approaches over the years. We have been developing an approach utilizing high-resolution...
NMR studies on the interactions between yeast Vta1 and Did2 during the multivesicular bodies sorting pathway.
Linear Mode
