5LGD

The CIDRa domain from MCvar1 PfEMP1 bound to CD36

Summary for 5LGD

• Entry DOI: 10.2210/pdb5lgd/pdb
• Descriptor: Platelet glycoprotein 4, PfEMP1 variant 1 of strain MC, alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
• Functional Keywords: plasmodium falciparum cytoadhesion scavenger receptor malaria, cell adhesion
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 2
• Total formula weight: 77593.83

Authors

Hsieh, F.L.,Higgins, M.K. (deposition date: 2016-07-06, release date: 2016-08-31, Last modification date: 2024-11-06)

Primary citation

Hsieh, F.L.,Turner, L.,Bolla, J.R.,Robinson, C.V.,Lavstsen, T.,Higgins, M.K.
The structural basis for CD36 binding by the malaria parasite.
Nat Commun, 7:12837-12837, 2016

PubMed Abstract: CD36 is a scavenger receptor involved in fatty acid metabolism, innate immunity and angiogenesis. It interacts with lipoprotein particles and facilitates uptake of long chain fatty acids. It is also the most common target of the PfEMP1 proteins of the malaria parasite, Plasmodium falciparum, tethering parasite-infected erythrocytes to endothelial receptors. This prevents their destruction by splenic clearance and allows increased parasitaemia. Here we describe the structure of CD36 in complex with long chain fatty acids and a CD36-binding PfEMP1 protein domain. A conserved hydrophobic pocket allows the hugely diverse PfEMP1 protein family to bind to a conserved phenylalanine residue at the membrane distal tip of CD36. This phenylalanine is also required for CD36 to interact with lipoprotein particles. By targeting a site on CD36 that is required for its physiological function, PfEMP1 proteins maintain the ability to tether to the endothelium and avoid splenic clearance.

PubMed: 27667267
DOI: 10.1038/ncomms12837

Experimental method

X-RAY DIFFRACTION (2.07 Å)