Source:http://linkedlifedata.com/resource/pubmed/id/16982608
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
46
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pubmed:dateCreated |
2006-11-13
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pubmed:databankReference | |
pubmed:abstractText |
Interleukin-10 receptor 2 (IL-10R2) is a critical component of the IL-10.IL-10R1.IL-10R2 complex which regulates IL-10-mediated immunomodulatory responses. The ternary IL-10 signaling complex is assembled in a sequential order with the IL-10.IL-10R1 interaction occurring first followed by engagement of the IL-10R2 chain. In this study we map the IL-10R2 binding site on IL-10 using surface plasmon resonance and cell-based assays. Critical IL-10R2 binding residues are located in helix A adjacent to the previously identified IL-10R1 recognition surface. Interestingly, IL-10R2 binding residues located in the N-terminal end of helix A exhibit large structural differences between unbound cIL-10 and cIL-10.IL-10R1 crystal structures. This suggests IL-10R1-induced conformational changes regulate IL-10R2 binding and assembly of the ternary IL-10.IL-10R1.IL-10R2 complex. The basic mechanistic features of the assembly process are likely shared by six additional class-2 cytokines (viral IL-10s, IL-22, IL-26, IL-28A, IL28B, and IL-29) to promote IL-10R2 binding to six additional receptor complexes. These studies highlight the importance of structure in regulating low affinity protein-protein interactions and IL-10 signal transduction.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
281
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
35088-96
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pubmed:dateRevised |
2007-12-3
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pubmed:meshHeading |
pubmed-meshheading:16982608-Amino Acid Sequence,
pubmed-meshheading:16982608-Animals,
pubmed-meshheading:16982608-Binding Sites,
pubmed-meshheading:16982608-Escherichia coli,
pubmed-meshheading:16982608-Interleukin-10,
pubmed-meshheading:16982608-Interleukin-10 Receptor beta Subunit,
pubmed-meshheading:16982608-Models, Molecular,
pubmed-meshheading:16982608-Molecular Sequence Data,
pubmed-meshheading:16982608-Protein Binding,
pubmed-meshheading:16982608-Protein Conformation,
pubmed-meshheading:16982608-Signal Transduction
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pubmed:year |
2006
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pubmed:articleTitle |
Conformational changes mediate interleukin-10 receptor 2 (IL-10R2) binding to IL-10 and assembly of the signaling complex.
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pubmed:affiliation |
Department of Microbiology and Center for Biophysical Sciences and Engineering, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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