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PDBsum entry 1y6m
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Immune system
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PDB id
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1y6m
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References listed in PDB file
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Key reference
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Title
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Same structure, Different function crystal structure of the epstein-Barr virus il-10 bound to the soluble il-10r1 chain.
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Authors
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S.I.Yoon,
B.C.Jones,
N.J.Logsdon,
M.R.Walter.
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Ref.
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Structure, 2005,
13,
551-564.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 2.
Figure 2. Viral and Human IL-10 Orientations and
Interdomain Angles
(A) hIL-10, (B) vIL-10, and (C) cmvIL-10
dimers bound to sIL-10R1 are shown. The interdomain angles of
each IL-10 are shown at the top of each complex. The rotations
(in degrees) of each IL-10 domain on the surface of sIL-10R1 are
denoted by arrows where the movement is from the circle to the
arrowhead. For cmvIL-10/sIL-10R1 complex, the rotation of each
sIL-10R1 relative to the hIL-10/sIL-10R1 complex is also shown.
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2005,
13,
551-564)
copyright 2005.
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