CD59

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 23: Line 23:
[[1erg]], [[1erh]], [[1cdq]], [[1cdr]], [[1cds]] – hCD59 extracellular domain – human - NMR<br />
[[1erg]], [[1erh]], [[1cdq]], [[1cdr]], [[1cds]] – hCD59 extracellular domain – human - NMR<br />
[[2ofs]], [[2j8b]], [[2uwr]], [[2ux2]] – hCD59 extracellular domain <br />
[[2ofs]], [[2j8b]], [[2uwr]], [[2ux2]] – hCD59 extracellular domain <br />
-
[[4bik]] – hCD59 extracellular domain + intermedilysin<br />
+
[[4bik]], [[5imt]] – hCD59 extracellular domain + intermedilysin<br />
 +
[[5imy]] – hCD59 extracellular domain + vaginolysin<br />
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 07:50, 30 March 2017

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

Drag the structure with the mouse to rotate

3D structures of CD59

Updated on 30-March-2017

1erg, 1erh, 1cdq, 1cdr, 1cds – hCD59 extracellular domain – human - NMR
2ofs, 2j8b, 2uwr, 2ux2 – hCD59 extracellular domain
4bik, 5imt – hCD59 extracellular domain + intermedilysin
5imy – hCD59 extracellular domain + vaginolysin

References

  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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

Personal tools