1D0G

CRYSTAL STRUCTURE OF DEATH RECEPTOR 5 (DR5) BOUND TO APO2L/TRAIL

Summary for 1D0G

• Entry DOI: 10.2210/pdb1d0g/pdb
• Descriptor: DEATH RECEPTOR-5, APOPTOSIS-2 LIGAND, ZINC ION, ... (5 entities in total)
• Functional Keywords: apoptosis, binding and specificity, ligand-receptor complex, tnf receptor family
• Biological source: Homo sapiens (human); More
• Cellular location: Membrane ; Single-pass type II membrane protein : P50591; Membrane; Single-pass type I membrane protein: O14763
• Total number of polymer chains: 6
• Total formula weight: 102398.38

Authors

Hymowitz, S.G.,Christinger, H.W.,Fuh, G.,O'Connell, M.P.,Kelley, R.F.,Ashkenazi, A.,de Vos, A.M. (deposition date: 1999-09-09, release date: 1999-10-22, Last modification date: 2024-10-16)

Primary citation

Hymowitz, S.G.,Christinger, H.W.,Fuh, G.,Ultsch, M.,O'Connell, M.,Kelley, R.F.,Ashkenazi, A.,de Vos, A.M.
Triggering cell death: the crystal structure of Apo2L/TRAIL in a complex with death receptor 5.
Mol.Cell, 4:563-571, 1999

PubMed Abstract: Formation of a complex between Apo2L (also called TRAIL) and its signaling receptors, DR4 and DR5, triggers apoptosis by inducing the oligomerization of intracellular death domains. We report the crystal structure of the complex between Apo2L and the ectodomain of DR5. The structure shows three elongated receptors snuggled into long crevices between pairs of monomers of the homotrimeric ligand. The interface is divided into two distinct patches, one near the bottom of the complex close to the receptor cell surface and one near the top. Both patches contain residues that are critical for high-affinity binding. A comparison to the structure of the lymphotoxin-receptor complex suggests general principles of binding and specificity for ligand recognition in the TNF receptor superfamily.

PubMed: 10549288
DOI: 10.1016/S1097-2765(00)80207-5

Experimental method

X-RAY DIFFRACTION (2.4 Å)