1y6m
From Proteopedia
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[[Image:1y6m.gif|left|200px]] | [[Image:1y6m.gif|left|200px]] | ||
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'''Crystal structure of Epstein-Barr virus IL-10 complexed with the soluble IL-10R1 chain''' | '''Crystal structure of Epstein-Barr virus IL-10 complexed with the soluble IL-10R1 chain''' | ||
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[[Category: Walter, M R.]] | [[Category: Walter, M R.]] | ||
[[Category: Yoon, S I.]] | [[Category: Yoon, S I.]] | ||
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- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:55:57 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 12:55, 3 May 2008
Crystal structure of Epstein-Barr virus IL-10 complexed with the soluble IL-10R1 chain
Overview
Human IL-10 (hIL-10) is a cytokine that modulates diverse immune responses. The Epstein-Barr virus (EBV) genome contains an IL-10 homolog (vIL-10) that shares high sequence and structural similarity with hIL-10. Although vIL-10 suppresses inflammatory responses like hIL-10, it cannot activate many other immunostimulatory functions performed by the cellular cytokine. These functional differences have been correlated with the approximately 1000-fold lower affinity of vIL-10, compared to hIL-10, for the IL-10R1 receptor chain. To define the structural basis for these observations, crystal structures of vIL-10 and a vIL-10 point mutant were determined bound to the soluble IL-10R1 receptor fragment (sIL-10R1) at 2.8 and 2.7 A resolution, respectively. The structures reveal that subtle changes in the conformation and dynamics of the vIL-10 AB and CD loops and an orientation change of vIL-10 on sIL-10R1 are the main factors responsible for vIL-10's reduced affinity for sIL-10R1 and its distinct biological profile.
About this Structure
1Y6M is a Protein complex structure of sequences from Homo sapiens and Human herpesvirus 4. Full crystallographic information is available from OCA.
Reference
Same structure, different function crystal structure of the Epstein-Barr virus IL-10 bound to the soluble IL-10R1 chain., Yoon SI, Jones BC, Logsdon NJ, Walter MR, Structure. 2005 Apr;13(4):551-64. PMID:15837194 Page seeded by OCA on Sat May 3 15:55:57 2008