1lqs
From Proteopedia
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| - | [[Image:1lqs.jpg|left|200px]] | + | [[Image:1lqs.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF HUMAN CYTOMEGALOVIRUS IL-10 BOUND TO SOLUBLE HUMAN IL-10R1''' | + | {{Structure |
| + | |PDB= 1lqs |SIZE=350|CAPTION= <scene name='initialview01'>1lqs</scene>, resolution 2.7Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF HUMAN CYTOMEGALOVIRUS IL-10 BOUND TO SOLUBLE HUMAN IL-10R1''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LQS is a [ | + | 1LQS is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Human_herpesvirus_5 Human herpesvirus 5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LQS OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12093920 12093920] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Human herpesvirus 5]] | [[Category: Human herpesvirus 5]] | ||
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[[Category: structure mimic]] | [[Category: structure mimic]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:34:03 2008'' |
Revision as of 10:34, 20 March 2008
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| , resolution 2.7Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF HUMAN CYTOMEGALOVIRUS IL-10 BOUND TO SOLUBLE HUMAN IL-10R1
Overview
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.
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
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