1du3: Difference between revisions
New page: left|200px<br /> <applet load="1du3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1du3, resolution 2.2Å" /> '''Crystal structure of... |
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[[Image:1du3.gif|left|200px]]<br /> | [[Image:1du3.gif|left|200px]]<br /><applet load="1du3" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1du3, resolution 2.2Å" /> | caption="1du3, resolution 2.2Å" /> | ||
'''Crystal structure of TRAIL-SDR5'''<br /> | '''Crystal structure of TRAIL-SDR5'''<br /> | ||
==Overview== | ==Overview== | ||
TRAIL is a cytokine that induces apoptosis in a wide variety of tumor | 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. | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1DU3 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1DU3 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DU3 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Cha, S | [[Category: Cha, S S.]] | ||
[[Category: Oh, B | [[Category: Oh, B H.]] | ||
[[Category: Sung, B | [[Category: Sung, B J.]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: complex]] | [[Category: complex]] | ||
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[[Category: trail]] | [[Category: trail]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:20:28 2008'' | ||
Revision as of 13:20, 21 February 2008
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Crystal structure of TRAIL-SDR5
OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Squamous cell carcinoma, head and neck OMIM:[603612]
About this StructureAbout this Structure
1DU3 is a Protein complex structure of sequences from Homo sapiens with as ligand. 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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