1du3: Difference between revisions

Revision as of 23:37, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1du3.png

Template:STRUCTURE 1du3

Crystal structure of TRAIL-SDR5Crystal structure of TRAIL-SDR5

Template:ABSTRACT PUBMED 10893238

About this StructureAbout this Structure

1DU3 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of TRAIL-DR5 complex identifies a critical role of the unique frame insertion in conferring recognition specificity., Cha SS, Sung BJ, Kim YA, Song YL, Kim HJ, Kim S, Lee MS, Oh BH, J Biol Chem. 2000 Oct 6;275(40):31171-7. PMID:10893238

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal structure of TRAIL-SDR5'''
+===Crystal structure of TRAIL-SDR5===
-==Overview==
+<!--
-TRAIL is a cytokine that induces apoptosis in a wide variety of tumor cells but rarely in normal cells. It contains an extraordinarily elongated loop because of an unique insertion of 12-16 amino acids compared with the other members of tumor necrosis factor family. Biological implication of the frame insertion has not been clarified. We have determined the crystal structure of TRAIL in a complex with the extracellular domain of death receptor DR5 at 2.2 A resolution. The structure reveals extensive contacts between the elongated loop and DR5 in an interaction mode that would not be allowed without the frame insertion. These interactions are missing in the structures of the complex determined by others recently. This observation, along with structure-inspired deletion analysis, identifies the critical role of the frame insertion as a molecular strategy conferring specificity upon the recognition of cognate receptors. The structure also suggests that a built-in flexibility of the tumor necrosis factor receptor family members is likely to play a general and important role in the binding and recognition of tumor necrosis factor family members.
+The line below this paragraph, {{ABSTRACT_PUBMED_10893238}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_10893238}}
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 [[Category: Dr5]]
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