Molecular simulations and solid-state NMR investigate dynamical structure in rhodopsin activation.

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Molecular simulations and solid-state NMR investigate dynamical structure in rhodopsin activation.

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MDD

NMR assignment:

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Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

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Amber

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Torsion angles from chemical shifts:

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TALOS

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

d2D

PECAN

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RCI

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HADDOCK

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Backbone S2

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B-factor

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Camshift

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ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

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Shifty

Camcoil

Poulsen_rc_CS

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08-20-2011, 03:31 PM

nmrlearner

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Molecular simulations and solid-state NMR investigate dynamical structure in rhodopsin activation.

Molecular simulations and solid-state NMR investigate dynamical structure in rhodopsin activation.

Molecular simulations and solid-state NMR investigate dynamical structure in rhodopsin activation.

Biochim Biophys Acta. 2011 Aug 8;

Authors: Mertz B, Struts AV, Feller SE, Brown MF

Abstract
Rhodopsin has served as the primary model for studying G protein-coupled receptors (GPCRs)-the largest group in the human genome, and consequently a primary target for pharmaceutical development. Understanding the functions and activation mechanisms of GPCRs has proven to be extraordinarily difficult, as they are part of a complex signaling cascade and reside within the cell membrane. Although X-ray crystallography has recently solved several GPCR structures that may resemble the activated conformation, the dynamics and mechanism of rhodopsin activation continue to remain elusive. Notably solid-state ((2))H NMR spectroscopy provides key information pertinent to how local dynamics of the retinal ligand change during rhodopsin activation. When combined with molecular mechanics simulations of proteolipid membranes, a new paradigm for the rhodopsin activation process emerges. Experiment and simulation both suggest that retinal isomerization initiates the rhodopsin photocascade to yield not a single activated structure, but rather an ensemble of activated conformational states. This article is part of a Special Issue entitled: Membrane protein structure and function.

PMID: 21851809 [PubMed - as supplied by publisher]

Source: PubMed

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