1lqs
From Proteopedia
(New page: 200px<br /> <applet load="1lqs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lqs, resolution 2.7Å" /> '''CRYSTAL STRUCTURE OF...) |
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caption="1lqs, resolution 2.7Å" /> | caption="1lqs, resolution 2.7Å" /> | ||
'''CRYSTAL STRUCTURE OF HUMAN CYTOMEGALOVIRUS IL-10 BOUND TO SOLUBLE HUMAN IL-10R1'''<br /> | '''CRYSTAL STRUCTURE OF HUMAN CYTOMEGALOVIRUS IL-10 BOUND TO SOLUBLE HUMAN IL-10R1'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LQS is a [http://en.wikipedia.org/wiki/Protein_complex 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] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1LQS is a [http://en.wikipedia.org/wiki/Protein_complex 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] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LQS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: structure mimic]] | [[Category: structure mimic]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:19:57 2008'' |
Revision as of 14:19, 15 February 2008
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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 with as ligand. 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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