2h24: Difference between revisions

Revision as of 20:47, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

2h24, resolution 2.00Å ()

Related:

1inr

Structural annotation:
Resources:	InterPro : Ipr000098, Ipr009079, Ipr012352, Ipr012351 Pfam : PF00726 UniProt : Q71UZ1

Functional annotation:
Cellular component:	extracellular region
Biological process:	immune response
Molecular function:	cytokine activity

Evolutionary conservation:

Toggle Conservation Colors:	Rows = identical sequences:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

Crystal structure of human IL-10Crystal structure of human IL-10

Template:ABSTRACT PUBMED 16982608

About this StructureAbout this Structure

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

ReferenceReference

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 Mon Jul 28 20:47:48 2008

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OCA

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-[[Image:2h24.gif|left|200px]]
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-'''Crystal structure of human IL-10'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16982608}}, adds the Publication Abstract to the page
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+-->
+{{ABSTRACT_PUBMED_16982608}}
 ==About this Structure==
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 [[Category: Yoon, S I.]]
 [[Category: Alpha-helix bundle]]
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