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. 2019 Nov 20;9:17123. doi: 10.1038/s41598-019-53388-8

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Pro191 and Ala252 are critically positioned to influence long chain fatty acid binding to CD36. The extracellular domain of human CD36 (pdb: 5lgd) is modelled in cartoon format showing the secondary structure with α-helices in cyan, β-strands in magenta and loops in salmon. The surface of the internal hydrophobic ‘Y’-shaped cavity is shown in transparent grey. The two palmitates modelled in the cavity are shown as ‘spheres’ and coloured orange (carbons) and red (oxygens). Pro191 and Ala252 are modelled in ‘spheres’ and coloured elementally with carbon in green, nitrogen in blue and oxygen in red. The three portals to the internal cavity are indicated by arrows. The grey arrow indicates a portal to the base and rear of the protein which is shown in close up from the perspective of the membrane in the bottom right panel. A close up of the upper right portal and the breaking of α-helix 8 by Pro191 is shown in the upper right panel.