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• (author = "Jensen, Morten" AND publisher = "National Academy of Sciences")
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author = "Jensen, Morten" > : "National Academy of Sciences" (x)
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Found 7 documents, displaying page 1 of 1

Energetics of glycerol conduction through aquaglyceroporin GlpF

Author(s) : Jensen, Morten Ø. , Park, Sanghyun , Tajkhorshid, Emad , Schulten, Klaus
Description : Aquaglyceroporin GlpF selectively conducts water and linear polyalcohols, such as glycerol, across the inner membrane of Escherichia coli. We report steered molecular dynamics simulations of glycerol conduction through GlpF, in which external forces accelerate the transchannel conduction in a manner...
Repository : Europe PubMed Central
Language(s) : English

Identification of two distinct inactive conformations of the β2-adrenergic receptor reconciles structural and biochemical observations

Author(s) : Dror, Ron O. , Arlow, Daniel H. , Borhani, David W. , Jensen, Morten Ø. , Piana, Stefano , Shaw, David E.
Description : Fully understanding the mechanisms of signaling proteins such as G protein-coupled receptors (GPCRs) will require the characterization of their conformational states and the pathways connecting those states. The recent crystal structures of the β2- and β1-adrenergic receptors in a nominally inactive...
Repository : Europe PubMed Central
Language(s) : English

Reply to Domene and Furini: Distinguishing knock-on and vacancy diffusion mechanisms

Author(s) : Jensen, Morten Ø. , Borhani, David W. , Lindorff-Larsen, Kresten , Dror, Ron O. , Shaw, David E.
Description :
Repository : Europe PubMed Central
Language(s) : English

Dynamic control of slow water transport by aquaporin 0: Implications for hydration and junction stability in the eye lens

Author(s) : Jensen, Morten Ø. , Dror, Ron O. , Xu, Huafeng , Borhani, David W. , Arkin, Isaiah T. , Eastwood, Michael P. , Shaw, David E.
Description : Aquaporin 0 (AQP0), the most abundant membrane protein in mammalian lens fiber cells, not only serves as the primary water channel in this tissue but also appears to mediate the formation of thin junctions between fiber cells. AQP0 is remarkably less water permeable than other aquaporins, but the st...
Repository : Europe PubMed Central
Language(s) : English

A conserved protonation-dependent switch controls drug binding in the Abl kinase

Author(s) : Shan, Yibing , Seeliger, Markus A. , Eastwood, Michael P. , Frank, Filipp , Xu, Huafeng , Jensen, Morten Ø , Dror, Ron O.
Description : In many protein kinases, a characteristic conformational change (the “DFG flip”) connects catalytically active and inactive conformations. Many kinase inhibitors—including the cancer drug imatinib—selectively target a specific DFG conformation, but the function and mechanism of the flip remain uncle...
Repository : Europe PubMed Central
Language(s) : English

Principles of conduction and hydrophobic gating in K+ channels

Author(s) : Jensen, Morten Ø. , Borhani, David W. , Lindorff-Larsen, Kresten , Maragakis, Paul , Jogini, Vishwanath , Eastwood, Michael P.
Description : We present the first atomic-resolution observations of permeation and gating in a K+ channel, based on molecular dynamics simulations of the Kv1.2 pore domain. Analysis of hundreds of simulated permeation events revealed a detailed conduction mechanism, resembling the Hodgkin–Keynes “knock-on” model...
Repository : Europe PubMed Central
Language(s) : English

Structural basis for inhibition of complement C5 by the SSL7 protein from Staphylococcus aureus

Author(s) : Laursen, Nick S. , Gordon, Natasha , Hermans, Stefan , Lorenz, Natalie , Jackson, Nicola , Wines, Bruce , Spillner, Edzard
Description : Staphylococcus aureus secretes the SSL7 protein as part of its immune evasion strategy. The protein binds both complement C5 and IgA, yet it is unclear whether SSL7 cross-links these two proteins and, if so, what purpose this serves the pathogen. We have isolated a stable IgA-SSL7-C5 complex, and o...
Repository : Europe PubMed Central
Language(s) : English
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Found 7 documents, displaying page 1 of 1