1d4v
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= TRANSIENT EXPRESSION AS IG FUSION PROTEIN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= TRANSIENT EXPRESSION AS IG FUSION PROTEIN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d4v OCA], [http://www.ebi.ac.uk/pdbsum/1d4v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1d4v RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==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. | 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. | ||
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| - | ==Disease== | ||
| - | Known disease associated with this structure: Squamous cell carcinoma, head and neck OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=603612 603612]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: trimeric jelly-roll]] | [[Category: trimeric jelly-roll]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:34:41 2008'' |
Revision as of 16:34, 30 March 2008
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| , resolution 2.2Å | |||||||
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| Gene: | TRANSIENT EXPRESSION AS IG FUSION PROTEIN (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of trail-DR5 complex
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.
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
Page seeded by OCA on Sun Mar 30 19:34:41 2008
