Editing CD36 (section)

=== Tertiary ===

Using [[Hydrophobicity scales|Kyte–Doolittle analysis]],<ref name="pmid7108955">{{cite journal | vauthors = Kyte J, Doolittle RF | title = A simple method for displaying the hydropathic character of a protein | journal = Journal of Molecular Biology | volume = 157 | issue = 1 | pages = 105–32 | date = May 1982 | pmid = 7108955 | doi = 10.1016/0022-2836(82)90515-0 | citeseerx = 10.1.1.458.454 }}</ref> the [[peptide sequence|amino acid sequence]] of CD36 predicts a [[hydrophobic]] region near each end of the protein large enough to span [[cell membrane|cellular membrane]]s. Based on this notion and the observation that CD36 is found on the surface of cells, CD36 is thought to have a 'hairpin-like' structure with [[alpha helix|α-helices]] at the C- and N- termini projecting through the [[cell membrane|membrane]] and a larger extracellular loop (Fig. 1). This [[membrane topology|topology]] is supported by transfection experiments in cultured cells using deletion mutants of CD36.<ref name="pmid10964685">{{cite journal | vauthors = Gruarin P, Thorne RF, Dorahy DJ, Burns GF, Sitia R, Alessio M | title = CD36 is a ditopic glycoprotein with the N-terminal domain implicated in intracellular transport | journal = Biochemical and Biophysical Research Communications | volume = 275 | issue = 2 | pages = 446–54 | date = August 2000 | pmid = 10964685 | doi = 10.1006/bbrc.2000.3333 }}</ref><ref name="pmid8798390">{{cite journal | vauthors = Tao N, Wagner SJ, Lublin DM | title = CD36 is palmitoylated on both N- and C-terminal cytoplasmic tails | journal = The Journal of Biological Chemistry | volume = 271 | issue = 37 | pages = 22315–20 | date = September 1996 | pmid = 8798390 | doi = 10.1074/jbc.271.37.22315 | doi-access = free }}</ref>

Based on the crystal structure of the homologous [[SCARB2]], a model of the extracellular domain of CD36 has been produced.<ref>{{cite journal | vauthors = Neculai D, Schwake M, Ravichandran M, Zunke F, Collins RF, Peters J, Neculai M, Plumb J, Loppnau P, Pizarro JC, Seitova A, Trimble WS, Saftig P, Grinstein S, Dhe-Paganon S | display-authors = 6 | title = Structure of LIMP-2 provides functional insights with implications for SR-BI and CD36 | journal = Nature | volume = 504 | issue = 7478 | pages = 172–6 | date = December 2013 | pmid = 24162852 | doi = 10.1038/nature12684 | bibcode = 2013Natur.504..172N | s2cid = 4395239 }}</ref> Like SCARB2, CD36 is proposed to contain an [[antiparallel (biochemistry)#Beta sheet|antiparallel]] β-barrel core with many short α-helices adorning it. The structure is predicted to contain a hydrophobic transport tunnel. 
Disulfide linkages between 4 of the 6 [[cysteine]] residues in the extracellular loop are required for efficient intracellular processing and transport of CD36 to the [[plasma membrane]].<ref name="pmid9371725">{{cite journal | vauthors = Gruarin P, Sitia R, Alessio M | title = Formation of one or more intrachain disulphide bonds is required for the intracellular processing and transport of CD36 | journal = The Biochemical Journal | volume = 328 | issue = 2 | pages = 635–42 | date = December 1997 | pmid = 9371725 | pmc = 1218965 | doi = 10.1042/bj3280635 }}</ref> It is not clear what role these linkages play on the function of the mature CD36 protein on the cell surface.