1d0g
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(New page: 200px<br /> <applet load="1d0g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d0g, resolution 2.4Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 14:20, 12 November 2007
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CRYSTAL STRUCTURE OF DEATH RECEPTOR 5 (DR5) BOUND TO APO2L/TRAIL
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Squamous cell carcinoma, head and neck OMIM:[603612]
About this Structure
1D0G is a Protein complex structure of sequences from Homo sapiens with ZN and CL as ligands. Full crystallographic information is available from OCA.
Reference
Triggering cell death: the crystal structure of Apo2L/TRAIL in a complex with death receptor 5., Hymowitz SG, Christinger HW, Fuh G, Ultsch M, O'Connell M, Kelley RF, Ashkenazi A, de Vos AM, Mol Cell. 1999 Oct;4(4):563-71. PMID:10549288
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