Stoichiometry of lipid interactions with transmembrane proteins--Deduced from the 3D structures.

Protein Science : a Publication of the Protein Society
T PáliDerek Marsh

Abstract

The stoichiometry of the first shell of lipids interacting with a transmembrane protein is defined operationally by the population of spin-labeled lipid chains whose motion is restricted directly by the protein. Interaction stoichiometries have been determined experimentally for a wide range of alpha-helical integral membrane proteins by using spin-label ESR spectroscopy. Here, we determine the spatially defined number of first-shell lipids at the hydrophobic perimeter of integral membrane proteins whose 3D structure has been determined by X-ray crystallography and lipid-protein interactions characterized by spin-labeling. Molecular modeling is used to build a single shell of lipids surrounding transmembrane structures derived from the PDB. Constrained energy optimization of the protein-lipid assemblies is performed by molecular mechanics. For relatively small proteins (up to 7-12 transmembrane helices), the geometrical first shell corresponds to that defined experimentally by perturbation of the lipid-chain dynamics. For larger, multi-subunit alpha-helical proteins, the lipids perturbed directly by the protein may either exceed or be less in number than those that can be accommodated at the intramembranous perimeter. In these ...Continue Reading

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Citations

Mar 2, 2016·Biochimica Et Biophysica Acta·Juan H BolivarAnthony Watts
Jul 20, 2007·Structure·John Holyoake, Mark S P Sansom
Jan 25, 2020·Biochimie·Sathishkumar MunusamyCarlos Munoz-Garay
Jul 6, 2012·Biochemistry·Juan H BolivarAnthony G Lee
Jul 2, 2019·The Journal of Physical Chemistry. B·Anusha KesireddyUlrich Kleinekathöfer
Feb 26, 2008·Biochimica Et Biophysica Acta·Derek Marsh
Aug 2, 2008·Methods : a Companion to Methods in Enzymology·Derek Marsh

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