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| | {{STRUCTURE_1lqs| PDB=1lqs | SCENE= }} | | {{STRUCTURE_1lqs| PDB=1lqs | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF HUMAN CYTOMEGALOVIRUS IL-10 BOUND TO SOLUBLE HUMAN IL-10R1'''
| + | ===CRYSTAL STRUCTURE OF HUMAN CYTOMEGALOVIRUS IL-10 BOUND TO SOLUBLE HUMAN IL-10R1=== |
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| - | ==Overview==
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| - | Human IL-10 (hIL-10) modulates critical immune and inflammatory responses by way of interactions with its high- (IL-10R1) and low-affinity (IL-10R2) cell surface receptors. Human cytomegalovirus exploits the IL-10 signaling pathway by expressing a functional viral IL-10 homolog (cmvIL-10), which shares only 27% sequence identity with hIL-10 yet signals through IL-10R1 and IL-10R2. To define the molecular basis of this virus-host interaction, we determined the 2.7-A crystal structure of cmvIL-10 bound to the extracellular fragment of IL-10R1 (sIL-10R1). The structure reveals cmvIL-10 forms a disulfide-linked homodimer that binds two sIL-10R1 molecules. Although cmvIL-10 and hIL-10 share similar intertwined topologies and sIL-10R1 binding sites, their respective interdomain angles differ by approximately 40 degrees. This difference results in a striking re-organization of the IL-10R1s in the putative cell surface complex. Solution binding studies show cmvIL-10 and hIL-10 share essentially identical affinities for sIL-10R1 whereas the Epstein-Barr virus IL-10 homolog (ebvIL-10), whose structure is highly similar to hIL-10, exhibits a approximately 20-fold reduction in sIL-10R1 affinity. Our results suggest cmvIL-10 and ebvIL-10 have evolved different molecular mechanisms to engage the IL-10 receptors that ultimately enhance the respective ability of their virus to escape immune detection.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12093920}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12093920 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12093920}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Receptor complex]] | | [[Category: Receptor complex]] |
| | [[Category: Structure mimic]] | | [[Category: Structure mimic]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:11:26 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 21:49:27 2008'' |
Revision as of 18:49, 2 July 2008
Template:STRUCTURE 1lqs
CRYSTAL STRUCTURE OF HUMAN CYTOMEGALOVIRUS IL-10 BOUND TO SOLUBLE HUMAN IL-10R1
Template:ABSTRACT PUBMED 12093920
About this Structure
1LQS is a Protein complex structure of sequences from Homo sapiens and Human herpesvirus 5. Full crystallographic information is available from OCA.
Reference
Crystal structure of human cytomegalovirus IL-10 bound to soluble human IL-10R1., Jones BC, Logsdon NJ, Josephson K, Cook J, Barry PA, Walter MR, Proc Natl Acad Sci U S A. 2002 Jul 9;99(14):9404-9. Epub 2002 Jul 1. PMID:12093920
Page seeded by OCA on Wed Jul 2 21:49:27 2008
