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| - | [[Image:1fg9.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1fg9| PDB=1fg9 | SCENE= }} | | {{STRUCTURE_1fg9| PDB=1fg9 | SCENE= }} |
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| - | '''3:1 COMPLEX OF INTERFERON-GAMMA RECEPTOR WITH INTERFERON-GAMMA DIMER'''
| + | ===3:1 COMPLEX OF INTERFERON-GAMMA RECEPTOR WITH INTERFERON-GAMMA DIMER=== |
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| - | ==Overview==
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| - | BACKGROUND: Molecular interactions among cytokines and cytokine receptors form the basis of many cell-signaling pathways relevant to immune function. Interferon-gamma (IFN-gamma) signals through a multimeric receptor complex consisting of two different but structurally related transmembrane chains: the high-affinity receptor-binding subunit (IFN-gammaRalpha) and a species-specific accessory factor (AF-1 or IFN-gammaRbeta). In the signaling complex, the two receptors probably interact with one another through their extracellular domains. Understanding the atomic interactions of signaling complexes enhances the ability to control and alter cell signaling and also provides a greater understanding of basic biochemical processes. RESULTS: The crystal structure of the complex of human IFN-gamma with the soluble, glycosylated extracellular part of IFN-gammaRalpha has been determined at 2.9 A resolution using multiwavelength anomalous diffraction methods. In addition to the expected 2:1 complex, the crystal structure reveals the presence of a third receptor molecule not directly associated with the IFN-gamma dimer. Two distinct intermolecular contacts, involving the edge strands of the C-terminal domains, are observed between this extra receptor and the 2:1 receptor-ligand complex thereby forming a 3:1 complex. CONCLUSIONS: The observed interactions in the 2:1 complex of the high-affinity cell-surface receptor with the IFN-gamma cytokine are similar to those seen in a previously reported structure where the receptor chains were not glycosylated. The formation of beta-sheet packing interactions between pairs of IFN-gammaRalpha receptors in these crystals suggests a possible model for receptor oligomerization of Ralpha and the structurally homologous Rbeta receptors in the fully active IFN-gamma signaling complex.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10986460}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10986460 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10986460}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Cytokine-receptor complex]] | | [[Category: Cytokine-receptor complex]] |
| | [[Category: Fibronectin type-iii]] | | [[Category: Fibronectin type-iii]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:17:24 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:12:11 2008'' |
Revision as of 00:12, 1 July 2008
Template:STRUCTURE 1fg9
3:1 COMPLEX OF INTERFERON-GAMMA RECEPTOR WITH INTERFERON-GAMMA DIMER
Template:ABSTRACT PUBMED 10986460
About this Structure
1FG9 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Observation of an unexpected third receptor molecule in the crystal structure of human interferon-gamma receptor complex., Thiel DJ, le Du MH, Walter RL, D'Arcy A, Chene C, Fountoulakis M, Garotta G, Winkler FK, Ealick SE, Structure. 2000 Sep 15;8(9):927-36. PMID:10986460
Page seeded by OCA on Tue Jul 1 03:12:11 2008
