科技报告详细信息
Molecular dynamics of membrane proteins.
Woolf, Thomas B. (Johns Hopkins University School of Medicine, Baltimore, MD) ; Crozier, Paul Stewart ; Stevens, Mark Jackson
Sandia National Laboratories
关键词: Gtp-Ases;    Membrane Proteins;    Stimuli;    Membrane Structures.;    59 Basic Biological Sciences;   
DOI  :  10.2172/919637
RP-ID  :  SAND2004-4962
RP-ID  :  AC04-94AL85000
RP-ID  :  919637
美国|英语
来源: UNT Digital Library
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【 摘 要 】

Understanding the dynamics of the membrane protein rhodopsin will have broad implications for other membrane proteins and cellular signaling processes. Rhodopsin (Rho) is a light activated G-protein coupled receptor (GPCR). When activated by ligands, GPCRs bind and activate G-proteins residing within the cell and begin a signaling cascade that results in the cell's response to external stimuli. More than 50% of all current drugs are targeted toward G-proteins. Rho is the prototypical member of the class A GPCR superfamily. Understanding the activation of Rho and its interaction with its Gprotein can therefore lead to a wider understanding of the mechanisms of GPCR activation and G-protein activation. Understanding the dark to light transition of Rho is fully analogous to the general ligand binding and activation problem for GPCRs. This transition is dependent on the lipid environment. The effect of lipids on membrane protein activity in general has had little attention, but evidence is beginning to show a significant role for lipids in membrane protein activity. Using the LAMMPS program and simulation methods benchmarked under the IBIG program, we perform a variety of allatom molecular dynamics simulations of membrane proteins.

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