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Biochim Biophys Acta. 2014 Jun;1838(6):1548-59. doi: 10.1016/j.bbamem.2013.11.009. Epub 2013 Nov 21.

Non-covalent binding of membrane lipids to membrane proteins.

Author information

1
Rutgers University Newark, 325 Hill Hall, 360 MLK Blvd, Newark, NJ 07102-1801, USA. Electronic address: pyeagle@andromeda.rutgers.edu.

Abstract

Polar lipids and membrane proteins are major components of biological membranes, both cell membranes and membranes of enveloped viruses. How these two classes of membrane components interact with each other to influence the function of biological membranes is a fundamental question that has attracted intense interest since the origins of the field of membrane studies. One of the most powerful ideas that driven the field is the likelihood that lipids bind to membrane proteins at specific sites, modulating protein structure and function. However only relatively recently has high resolution structure determination of membrane proteins progressed to the point of providing atomic level structure of lipid binding sites on membrane proteins. Analysis of X-ray diffraction, electron crystallography and NMR data over 100 specific lipid binding sites on membrane proteins. These data demonstrate tight lipid binding of both phospholipids and cholesterol to membrane proteins. Membrane lipids bind to membrane proteins by their headgroups, or by their acyl chains, or binding is mediated by the entire lipid molecule. When headgroups bind, binding is stabilized by polar interactions between lipid headgroups and the protein. When acyl chains bind, van der Waals effects dominate as the acyl chains adopt conformations that complement particular sites on the rough protein surface. No generally applicable motifs for binding have yet emerged. Previously published biochemical and biophysical data link this binding with function. This Article is Part of a Special Issue Entitled: Membrane Structure and Function: Relevance in the Cell's Physiology, Pathology and Therapy.

KEYWORDS:

Lipid binding site; Lipid–protein interaction; NMR; X-ray diffraction

PMID:
24269542
DOI:
10.1016/j.bbamem.2013.11.009
[Indexed for MEDLINE]
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