2UX2

High resolution structure of human CD59

Summary for 2UX2

• Entry DOI: 10.2210/pdb2ux2/pdb
• Related: 1CDQ 1CDR 1CDS 1ERG 1ERH 2J8B 2UWR
• Descriptor: CD59 GLYCOPROTEIN (2 entities in total)
• Functional Keywords: mac, mirl, cd59, membrane, gpi-anchor, lipoprotein, glycoprotein, complement regulator, immune system
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cell membrane; Lipid-anchor, GPI-anchor: P13987
• Total number of polymer chains: 3
• Total formula weight: 27303.91

Authors

Leath, K.J.,Johnson, S.,Roversi, P.,Morgan, B.P.,Smith, R.A.G.,Lea, S.M. (deposition date: 2007-03-26, release date: 2007-08-07, Last modification date: 2024-11-13)

Primary citation

Leath, K.J.,Johnson, S.,Roversi, P.,Hughes, T.R.,Smith, R.A.G.,Mackenzie, L.,Morgan, B.P.,Lea, S.M.
High-Resolution Structures of Bacterially Expressed Soluble Human Cd59.
Acta Crystallogr.,Sect.F, 63:648-, 2007

PubMed Abstract: CD59 is a membrane-bound glycoprotein that protects host cells from lysis by inhibiting the terminal pathway of complement, preventing the formation and insertion of the membrane attack complex (MAC). Crystals of bacterially expressed and nonglycosylated recombinant soluble human CD59 have been obtained from three crystallization conditions, each of which gave rise to a distinct crystal form. Each crystal form led to a crystal structure at high resolution (1.15, 1.35 and 1.8 A). In one of these structures the electron-density map shows an as yet unidentified small molecule in the predicted C8/C9-binding site. The presence/absence of this ligand is linked to alternate conformations of the amino acids implicated in C8/C9 binding.

PubMed: 17671359
DOI: 10.1107/S1744309107033477

Experimental method

X-RAY DIFFRACTION (1.8 Å)