2h24

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[[Image:2h24.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2h24 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h24 OCA], [http://www.ebi.ac.uk/pdbsum/2h24 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2h24 RCSB]</span>
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'''Crystal structure of human IL-10'''
'''Crystal structure of human IL-10'''
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[[Category: Walter, M R.]]
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[[Category: Yoon, S I.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:46:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:24:24 2008''
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Revision as of 02:46, 4 May 2008

Image:2h24.gif


PDB ID 2h24

Drag the structure with the mouse to rotate
2h24, resolution 2.00Å ()
Related: 1inr
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of human IL-10


Overview

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.

About this Structure

2H24 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Conformational changes mediate interleukin-10 receptor 2 (IL-10R2) binding to IL-10 and assembly of the signaling complex., Yoon SI, Logsdon NJ, Sheikh F, Donnelly RP, Walter MR, J Biol Chem. 2006 Nov 17;281(46):35088-96. Epub 2006 Sep 18. PMID:16982608 Page seeded by OCA on Sun May 4 05:46:53 2008

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