Structure of IL-22 bound to its high-affinity IL-22R1 chain (Q24656543)

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• Structure of IL-22 Bound to Its High-Affinity IL-22R1 Chain

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Language	Label	Description	Also known as
English	Structure of IL-22 bound to its high-affinity IL-22R1 chain	scientific article	Structure of IL-22 Bound to Its High-Affinity IL-22R1 Chain

Statements

instance of

scholarly article

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title

Structure of IL-22 bound to its high-affinity IL-22R1 chain (English)

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main subject

structural biology

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author name string

Brandi C Jones

series ordinal

1

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Naomi J Logsdon

series ordinal

2

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Mark R Walter

series ordinal

3

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language of work or name

English

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publication date

10 September 2008

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published in

Structure

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volume

16

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issue

9

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page(s)

1333-44

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cites work

Interleukin (IL)-22 and IL-17 are coexpressed by Th17 cells and cooperatively enhance expression of antimicrobial peptides

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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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A soluble class II cytokine receptor, IL-22RA2, is a naturally occurring IL-22 antagonist

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Identification, cloning, and characterization of a novel soluble receptor that binds IL-22 and neutralizes its activity

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Cloning and characterization of IL-22 binding protein, a natural antagonist of IL-10-related T cell-derived inducible factor/IL-22

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Human interleukin-10-related T cell-derived inducible factor: molecular cloning and functional characterization as an hepatocyte-stimulating factor

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Interleukin (IL)-22, a novel human cytokine that signals through the interferon receptor-related proteins CRF2-4 and IL-22R

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7 April 2017

Identification and functional characterization of a second chain of the interleukin-10 receptor complex

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7 April 2017

Crystal structure of recombinant human interleukin-22

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7 April 2017

Crystal structure of the IL-10/IL-10R1 complex reveals a shared receptor binding site

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7 April 2017

Crystal structure of interleukin-10 reveals the functional dimer with an unexpected topological similarity to interferon gamma

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7 April 2017

Crystal structure of interleukin 10 reveals an interferon gamma-like fold

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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VMD: visual molecular dynamics

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Improved methods for building protein models in electron density maps and the location of errors in these models

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7 April 2017

Comparison of interleukin-22 and interleukin-10 soluble receptor complexes

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7 April 2017

IL-22 increases the innate immunity of tissues

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Interleukin-10 and related cytokines and receptors

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7 April 2017

Cloning and characterization of mouse IL-22 binding protein

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7 April 2017

Cutting edge: STAT activation by IL-19, IL-20 and mda-7 through IL-20 receptor complexes of two types

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7 April 2017

Interleukin 20: discovery, receptor identification, and role in epidermal function

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7 April 2017

Ribbons

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7 April 2017

Interleukin-22 mediates early host defense against attaching and effacing bacterial pathogens

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7 April 2017

Multiple protein sequence alignment from tertiary structure comparison: assignment of global and residue confidence levels

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Crystallization and preliminary X-ray diffraction analysis of human IL-22 bound to the extracellular IL-22R1 chain

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IL-22 mediates mucosal host defense against Gram-negative bacterial pneumonia

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28 September 2017

IL-22 is required for Th17 cell-mediated pathology in a mouse model of psoriasis-like skin inflammation

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28 September 2017

Interleukin-22 forms dimers that are recognized by two interleukin-22R1 receptor chains

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28 September 2017

Interleukin-22 but not interleukin-17 provides protection to hepatocytes during acute liver inflammation

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28 September 2017

Model for growth hormone receptor activation based on subunit rotation within a receptor dimer

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28 September 2017

Interleukin 22 (IL-22) plays a protective role in T cell-mediated murine hepatitis: IL-22 is a survival factor for hepatocytes via STAT3 activation

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28 September 2017

Expression patterns of IL-10 ligand and receptor gene families provide leads for biological characterization.

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28 September 2017

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28 September 2017

Interleukin-22 (IL-22) activates the JAK/STAT, ERK, JNK, and p38 MAP kinase pathways in a rat hepatoma cell line. Pathways that are shared with and distinct from IL-10.

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28 September 2017

Differential IL-10R1 expression plays a critical role in IL-10-mediated immune regulation

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28 September 2017

Identification of the functional interleukin-22 (IL-22) receptor complex: the IL-10R2 chain (IL-10Rbeta ) is a common chain of both the IL-10 and IL-22 (IL-10-related T cell-derived inducible factor, IL-TIF) receptor complexes

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28 September 2017

Cloning and characterization of IL-10-related T cell-derived inducible factor (IL-TIF), a novel cytokine structurally related to IL-10 and inducible by IL-9.

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28 September 2017

CLAMP: a biosensor kinetic data analysis program

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28 September 2017

Conformational changes mediate interleukin-10 receptor 2 (IL-10R2) binding to IL-10 and assembly of the signaling complex

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IL-22 induces lipopolysaccharide-binding protein in hepatocytes: a potential systemic role of IL-22 in Crohn's disease.

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Interactions among the components of the interleukin-10 receptor complex

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28 November 2018

Structure of insect-cell-derived IL-22.

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The IL-10R2 binding hot spot on IL-22 is located on the N-terminal helix and is dependent on N-linked glycosylation

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28 November 2018

Erythropoietin receptor activation by a ligand-induced conformation change

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A role for T cell-derived interleukin 22 in psoriatic skin inflammation

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12 December 2020

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Interleukin (IL)-19, IL-20 and IL-24 are produced by and act on keratinocytes and are distinct from classical ILs

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https://pubmed.ncbi.nlm.nih.gov/18599299

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The Effects of IL-20 Subfamily Cytokines on Reconstituted Human Epidermis Suggest Potential Roles in Cutaneous Innate Defense and Pathogenic Adaptive Immunity in Psoriasis

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IL-22 regulates the expression of genes responsible for antimicrobial defense, cellular differentiation, and mobility in keratinocytes: a potential role in psoriasis

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https://pubmed.ncbi.nlm.nih.gov/18599299

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based on heuristic

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Identifiers

DOI

10.1016/J.STR.2008.06.005

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

685056

OpenCitations bibliographic resource ID

685056

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

685056

PMC publication ID

2637415

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

685056

PubMed publication ID

18599299

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

685056

ResearchGate publication ID

5252691

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