Structure of IL-22 bound to its high-affinity IL-22R1 chain.
Structure of IL-22 bound to its high-affinity IL-22R1 chain.
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DOI：
10.1016/j.str.2008.06.005
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发表时间：
2008-09-10
期刊：
影响因子：
5.7
通讯作者：
Walter, Mark R.
中科院分区：
文献类型：
--
作者：
Jones, Brandi C.;Logsdon, Naomi J.;Walter, Mark R.
IL-22 is an IL-10 family cytokine that initiates innate immune responses against bacterial pathogens and contributes to immune disease. IL-22 biological activity is initiated by binding to a cell surface complex composed IL-22R1 and IL-10R2 receptor chains and further regulated by interactions with a soluble binding protein, IL-22BP, which shares sequence similarity with extracellular region of IL-22R1 (sIL-22R1). IL-22R1 also pairs with the IL-20R2 chain to induce IL-20 and IL-24 signaling. To define the molecular basis of these diverse interactions, we have determined structure of the IL-22/sIL-22R1 complex. The structure, combined with homology modeling and surface plasmon resonance studies, define the molecular basis for the distinct affinities and specificities of IL-22 and IL-10 receptor chains that regulate cellular targeting and signal transduction to elicit effective immune responses.
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影响因子：
14.9
作者：
Eswar, N;John, B;Sali, A
通讯作者：
Sali, A
影响因子：
4.6
作者：
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影响因子：
4.4
作者：
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Pestka, S
DOI：
10.1107/s0907444998003254
发表时间：
1998-09-01
期刊：
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
影响因子：
--
作者：
Brunger, AT;Adams, PD;Warren, GL
通讯作者：
Warren, GL
影响因子：
4.4
作者：
Dumoutier, L;Lejeune, D;Renauld, JC
通讯作者：
Renauld, JC