1d4v

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[[Image:1d4v.gif|left|200px]]
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{{STRUCTURE_1d4v| PDB=1d4v | SCENE= }}
{{STRUCTURE_1d4v| PDB=1d4v | SCENE= }}
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'''Crystal structure of trail-DR5 complex'''
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===Crystal structure of trail-DR5 complex===
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==Overview==
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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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(as it appears on PubMed at http://www.pubmed.gov), where 10542098 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10542098}}
==About this Structure==
==About this Structure==
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[[Category: Tnf-r superfamily]]
[[Category: Tnf-r superfamily]]
[[Category: Trimeric jelly-roll]]
[[Category: Trimeric jelly-roll]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:27:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:25:28 2008''

Revision as of 19:25, 30 June 2008

Image:1d4v.png

Template:STRUCTURE 1d4v

Crystal structure of trail-DR5 complex

Template:ABSTRACT PUBMED 10542098

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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