3QO4

The Crystal Structure of Death Receptor 6

Summary for 3QO4

• Entry DOI: 10.2210/pdb3qo4/pdb
• Descriptor: Tumor necrosis factor receptor superfamily member 21, ACETATE ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: tumor necrosis factor receptor (tnfr), apoptosis, alzheimer s disease, ligand-receptor-recognition
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Single-pass type I membrane protein (Probable): O75509
• Total number of polymer chains: 1
• Total formula weight: 19803.55

Authors

Kuester, M.,Kemmerzehl, S.,Dahms, S.O.,Roeser, D.,Than, M.E. (deposition date: 2011-02-09, release date: 2011-05-18, Last modification date: 2024-10-16)

Primary citation

Kuester, M.,Kemmerzehl, S.,Dahms, S.O.,Roeser, D.,Than, M.E.
The crystal structure of death receptor 6 (DR6): a potential receptor of the amyloid precursor protein (APP).
J.Mol.Biol., 409:189-201, 2011

PubMed Abstract: Death receptors belong to the tumor necrosis factor receptor (TNFR) super family and are intimately involved in the signal transduction during apoptosis, stress response and cellular survival. Here we present the crystal structure of recombinantly expressed death receptor six (DR6), one family member that was recently shown to bind to the amyloid precursor protein (APP) and hence to be probably involved in the development of Alzheimer's disease. The extracellular cysteine rich region of DR6, the typical ligand binding region of all TNFRs, was refined to 2.2 Å resolution and shows that its four constituting cysteine rich domains (CRDs) are arranged in a rod-like overall structure, which presents DR6-specific surface patches responsible for the exclusive recognition of its ligand(s). Based on the structural data, the general ligand binding modes of TNFRs and molecular modeling experiments we were able to elucidate structural features of the potential DR6-APP signaling complex.

PubMed: 21463639
DOI: 10.1016/j.jmb.2011.03.048

Experimental method

X-RAY DIFFRACTION (2.2 Å)