Membrane proteins bind lipids selectively to modulate their structure and function.

Journal article

Previous studies have established that the folding, structure and function of membrane proteins are influenced by their lipid environments and that lipids can bind to specific sites, for example, in potassium channels. Fundamental questions remain however regarding the extent of membrane protein selectivity towards lipids. Here we report a mass spectrometry approach designed to determine the selectivity of lipid binding to membrane protein complexes. We investigate the mechanosensitive channe...

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Authors: Laganowsky, A; Reading, E; Allison, T; Ulmschneider, M; Degiacomi, M

• Publication status: Published
• Journal: Nature
• Volume: 510
• Issue: 7503
• Pages: 172-175
• Publication date: 2014-06-01
• DOI: 10.1038/nature13419
• EISSN: 1476-4687
• ISSN: 0028-0836
• Language: English
• Keywords: Apoproteins; Cation Transport Proteins; Escherichia coli; Aquaporins; Bacterial Proteins; Protein Folding; Substrate Specificity; Phosphatidylglycerols; Membrane Proteins; Ion Channels; Crystallography, X-Ray; Lipid Bilayers; Ammonia; Membrane Lipids; Mass Spectrometry; Protein Stability; Cardiolipins; Protein Conformation; Escherichia coli Proteins; Mycobacterium tuberculosis; Protein Unfolding; Models, Molecular