1d0g: Difference between revisions

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[[Image:1d0g.gif|left|200px]]
{{Seed}}
[[Image:1d0g.png|left|200px]]


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{{STRUCTURE_1d0g|  PDB=1d0g  |  SCENE=  }}  
{{STRUCTURE_1d0g|  PDB=1d0g  |  SCENE=  }}  


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




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_10549288}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 10549288 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10549288}}


==About this Structure==
==About this Structure==
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[[Category: Ligand-receptor complex]]
[[Category: Ligand-receptor complex]]
[[Category: Tnf receptor family]]
[[Category: Tnf receptor family]]
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