Abstract
The most probable interlocation of transmembrane α-helices of Na+, K+-ATPase has been calculated by a computer-aided molecular simulation approach in the framework of models with eight and 10 helical peptides for the α-subunit. The method is based on the concept of three-dimensional molecular hydrophobicity potential (MHP) and provides valuable description of spatial hydrophobic properties of membrane-spanning segments as well as helix-helix packing interactions inside the membrane. Resulting model of the arrangement of intramembrane domain agrees with recent results on hydrophobic photolabeling of an intramembrane part of the β-subunit and the sixth transmembrane segment of the α-subunit. It is also consistent with current ideas on hydrophobic organization of integral membrane proteins. Possible topology of a cation-binding site is discussed.
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Efremov, R.G., Gulyaev, D.I. & Modyanov, N.N. Application of three-dimensional molecular hydrophobicity potential to the analysis of spatial organization of membrane domains in proteins. III. Modeling of intramembrane moiety of Na+, K+-ATPase. J Protein Chem 12, 143–152 (1993). https://doi.org/10.1007/BF01026035
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DOI: https://doi.org/10.1007/BF01026035