CD59

Function

CD59 (Cluster of Differentiation 59) is a protein which attaches to host cells via a GPI anchor. CD59 can prevent the formation of complement membrane attack complex via binding to complement C8 or C9. ^[1]

Relevance

HIV, vaccinia and cytomegalovirus incorporate human CD59 into their envelope thus preventing their lysis by complement.

Disease

Mutations in CD59 causes disease involving thrombosis.

Structural highlights

^[2].

Structure of human CD59 extracellular domain (green) complex with intermedilysin (cyan) (PDB entry 4bik)

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3D structures of CD593D structures of CD59

Updated on 20-January-2025

1erg, 1erh, 1cdq, 1cdr, 1cds – hCD59 extracellular domain 26-102 – human - NMR
2ofs, 2j8b, 2uwr, 2ux2 – hCD59 extracellular domain
8cn6 – hCD59 extracellular domain + cyclic peptide
4bik, 5imt – hCD59 extracellular domain + intermedilysin
5imy – hCD59 extracellular domain + vaginolysin
6zd0 – hCD59 extracellular domain + cytolysin – Cryo EM
8b0f – hCD59 extracellular domain + C5b8 – Cryo EM
8b0g, 8b0h – hCD59 extracellular domain + C5b9 + 2C9 – Cryo EM

ReferencesReferences

↑ Meri S, Morgan BP, Davies A, Daniels RH, Olavesen MG, Waldmann H, Lachmann PJ. Human protectin (CD59), an 18,000-20,000 MW complement lysis restricting factor, inhibits C5b-8 catalysed insertion of C9 into lipid bilayers. Immunology. 1990 Sep;71(1):1-9. PMID:1698710
↑ Johnson S, Brooks NJ, Smith RA, Lea SM, Bubeck D. Structural Basis for Recognition of the Pore-Forming Toxin Intermedilysin by Human Complement Receptor CD59. Cell Rep. 2013 May 30;3(5):1369-77. doi: 10.1016/j.celrep.2013.04.029. Epub 2013 , May 9. PMID:23665225 doi:10.1016/j.celrep.2013.04.029

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

[1] Meri S, Morgan BP, Davies A, Daniels RH, Olavesen MG, Waldmann H, Lachmann PJ. Human protectin (CD59), an 18,000-20,000 MW complement lysis restricting factor, inhibits C5b-8 catalysed insertion of C9 into lipid bilayers. Immunology. 1990 Sep;71(1):1-9. PMID:1698710

[2] Johnson S, Brooks NJ, Smith RA, Lea SM, Bubeck D. Structural Basis for Recognition of the Pore-Forming Toxin Intermedilysin by Human Complement Receptor CD59. Cell Rep. 2013 May 30;3(5):1369-77. doi: 10.1016/j.celrep.2013.04.029. Epub 2013 , May 9. PMID:23665225 doi:10.1016/j.celrep.2013.04.029

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