Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Volume 1818, Issue 12, Pages 2936-2942Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamem.2012.07.032
Keywords
Human serotonin(1A) receptor; Cholesterol; Ligand binding; Thermal deactivation; Fluorescence anisotropy
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Funding
- Council of Scientific and Industrial Research, Govt. of India
- Council of Scientific and Industrial Research
- Department of Science and Technology, Government of India
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A number of recently solved crystal structures of G-protein coupled receptors reveal the presence of closely associated cholesterol molecules in the receptor structure. We have previously shown the requirement of membrane cholesterol in the organization, dynamics and function of the serotonin(1A) receptor, a representative G-protein coupled receptor. In this work, we explored the role of membrane cholesterol in the stability of the human serotonin(1A) receptor. Analysis of sensitivity of the receptor to thermal deactivation, pH, and proteolytic digestion in control, cholesterol-depleted and cholesterol-enriched membranes comprehensively demonstrate that membrane cholesterol stabilizes the serotonin(1A) receptor. We conclude that these results could have potential implications in future efforts toward crystallizing the receptor. (C) 2012 Elsevier B.V. All rights reserved.
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