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Your search keyword '"Doris Nguyen"' showing total 3 results
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3 results on '"Doris Nguyen"'

1. ESCRT ubiquitin-binding domains function cooperatively during MVB cargo sorting

Author

Doris Nguyen, Robert C. Piper, S. Brookhart Shields, Stanley C. Winistorfer, Johanna A. Payne, Andrea J. Oestreich, and David J. Katzmann

Subjects
Binding Sites, Ubiquitin binding, Ubiquitin, Endosome, Endosomes, macromolecular substances, Cell Biology, Plasma protein binding, Biology, ESCRT, Cell biology, Transport protein, ESCRT complex, Protein Transport, Report, Multiprotein Complexes, biology.protein, Vesicular Transport Proteins, Animals, Humans, Research Articles, Protein Binding
Abstract

Ubiquitin (Ub) sorting receptors facilitate the targeting of ubiquitinated membrane proteins into multivesicular bodies (MVBs). Ub-binding domains (UBDs) have been described in several endosomal sorting complexes required for transport (ESCRT). Using available structural information, we have investigated the role of the multiple UBDs within ESCRTs during MVB cargo selection. We found a novel UBD within ESCRT-I and show that it contributes to MVB sorting in concert with the known UBDs within the ESCRT complexes. These experiments reveal an unexpected level of coordination among the ESCRT UBDs, suggesting that they collectively recognize a diverse set of cargo rather than act sequentially at discrete steps.

Published
2009
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2. Crystal Structure of the Bromide-Bound D85S Mutant of Bacteriorhodopsin: Principles of Ion Pumping

Author

Shahab Rouhani, Marc T. Facciotti, Doris Nguyen, Robert M. Glaeser, and Vincent S. Cheung

Subjects
Bromides, Models, Molecular, Protein Conformation, Surface Properties, Molecular Conformation, Biophysics, Ion Pumps, Crystal structure, Crystallography, X-Ray, Ion, Cell membrane, Structure-Activity Relationship, chemistry.chemical_compound, Protein structure, Bromide, Proton transport, medicine, Computer Simulation, Photobiophysics, Binding Sites, biology, Chemistry, Bacteriorhodopsin, Protein Structure, Tertiary, Crystallography, medicine.anatomical_structure, Models, Chemical, Ion pump, Bacteriorhodopsins, Mutation, Solvents, biology.protein, Protein Binding
Abstract

We report the crystal structure of a bromide-bound form of the D85S mutant of bacteriorhodopsin, bR(D85S), a protein that uses light energy rather than ATP to pump halide ions across the cell membrane. Comparison of the structure of the halide-bound and halide-free states reveals that both displacements of individual side-chain positions and concerted helical movements occur on the extracellular side of the protein. Analysis of these structural changes reveals how this ion pump first facilitates ion uptake deep within the cell membrane and then prevents the backward escape of ions later in the pumping cycle. Together with the information provided by structures of intermediate states in the bacteriorhodopsin photocycle, this study also suggests the overall design principles that are necessary for ion pumping.

Published
2003
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3. Crystallization of membrane proteins from media composed of connected-bilayer gels

Author

Shahab Rouhani, Doris Nguyen, Christian Cunningham, Glenna Woodcock, Robert M. Glaeser, Chiann-Tso Lin, Behzad Rad, Marc T. Facciotti, Christopher S. Lunde, and Vincent S. Cheung

Subjects
Halobacterium, Models, Molecular, Protein Conformation, Lipid Bilayers, Molecular Conformation, Biophysics, Crystallography, X-Ray, Biochemistry, law.invention, Biomaterials, Membrane Lipids, law, Crystallization, biology, Chemistry, Bilayer, Organic Chemistry, Membrane Proteins, Bacteriorhodopsin, General Medicine, Culture Media, Crystallography, Membrane protein, Bacteriorhodopsins, biology.protein, Thermodynamics, Gels
Abstract

The use of hydrated-lipid gels in which the bilayer is an infinitely periodic (or at least continuous), three-dimensional structure offers a relatively new approach for the crystallization of membrane proteins. While excellent crystals of the Halobacterial rhodopsins have been obtained with such media, success remains poor in extending their use to other membrane proteins. Experience with crystallization of bacteriorhodopsin has led us to recognize a number of improvements that can be made in the use of such hydrated-gel media, which may now prove to be of general value for the crystallization of other membrane proteins. © 2003 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 66: 300–316, 2002

Published
2002
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