The class B scavenger receptor CD36 is a driving force in pathological events, such as malarial infection, platelet-induced thrombus formation, and macrophage lipid loading during atherogenesis, as well as physiological events involving fatty acid transport. The mechanisms underlying these and other functions of CD36 have not been fully defined at the structural level, largely because previous studies were limited by the lack of a high-resolution CD36 structure. Recently, a high-resolution,

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... e-dimensional structure of the CD36 extracellular domain was determined by X-ray crystallography. This new structural information necessitates a review of past literature to determine how reported structural features fit into the newly solved structure. In this review, we provide the first comprehensive summary of known structural features of CD36 within the context of its newly solved three-dimensional structure. Importantly, the CD36 structure confirms the presence of one or more hydrophobic channels within the extracellular domain that likely function to transport fatty acids and, potentially, cholesterol. While the extracellular CD36 structure greatly enhances our mechanistic understanding of ligand binding and transport, a full-length structure that includes the transmembrane and intracellular domains will be critical to understand the positioning of CD36 on the plasma membrane and how it may interact with other proteins. Nonetheless, the current solved structure builds on our previous understanding of CD36 ligand binding sites and post-translational modifications and paves the way for future mechanistic studies to better understand CD36 function. In this review, we emphasize structural features relevant to platelet biology, highlighting new insights and suggesting additional areas of study into CD36 structure-function relationships.