1d4v
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(New page: 200px<br /> <applet load="1d4v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d4v, resolution 2.2Å" /> '''Crystal structure of...)
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Revision as of 14:22, 12 November 2007
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Crystal structure of trail-DR5 complex
Contents |
Overview
TRAIL, an apoptosis inducing ligand, has at least four cell surface, receptors including the death receptor DR5. Here we report the crystal, structure at 2.2 A resolution of a complex between TRAIL and the, extracellular region of DR5. TRAIL forms a central homotrimer around which, three DR5 molecules bind. Radical differences in the surface charge of the, ligand, together with variation in the alignment of the two receptor, domains confer specificity between members of these ligand and receptor, families. The existence of a switch mechanism allowing variation in, receptor domain alignment may mean that it is possible to engineer, receptors with multiple specificities by exploiting contact positions, unique to individual receptor-ligand pairs.
Disease
Known disease associated with this structure: Squamous cell carcinoma, head and neck OMIM:[603612]
About this Structure
1D4V is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the TRAIL-DR5 complex reveals mechanisms conferring specificity in apoptotic initiation., Mongkolsapaya J, Grimes JM, Chen N, Xu XN, Stuart DI, Jones EY, Screaton GR, Nat Struct Biol. 1999 Nov;6(11):1048-53. PMID:10542098
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