Structural Model of the Oncostatin M (OSM)-OSMRβ-gp130 TernaryComplex Reveals Pathways of Allosteric Communication in OSMSignaling

The findings of this study not only enhance the mechanistic understanding of OSM binding to the heteromeric OSMRβ/gp130 but also identify druggable binding sites for structure-based design of small molecules to inhibit the intracellular signal transduction.

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Publication Details

Journal
Current Medicinal Chemistry
Published
2025-07-01
DOI
https://doi.org/10.2174/0109298673362742250508113436
Citations
1
Primary Topic
Cytokine Signaling Pathways and Interactions
Type
article
Field-Weighted Citation Impact
1.05
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article

Structural Model of the Oncostatin M (OSM)-OSMRβ-gp130 TernaryComplex Reveals Pathways of Allosteric Communication in OSMSignaling

Weiwei Xue, Ding Luo, Qian Yan, Qingqing Du
1 citations
Current Medicinal Chemistry
Cytokine Signaling Pathways and Interactions
1.05
article

Structural Model of the Oncostatin M (OSM)-OSMRβ-gp130 TernaryComplex Reveals Pathways of Allosteric Communication in OSMSignaling

Weiwei Xue, Ding Luo, Qian Yan, Qingqing Du
article en
1 citations

Abstract

The findings of this study not only enhance the mechanistic understanding of OSM binding to the heteromeric OSMRβ/gp130 but also identify druggable binding sites for structure-based design of small molecules to inhibit the intracellular signal transduction.

Current Medicinal ChemistryVol. 32
Chongqing University (CN), Dalian Medical University (CN), Second Affiliated Hospital of Chongqing Medical University (CN), Chongqing Medical University (CN)
Good health and well-being
Openalex Percentile: Top 20%
Cytokine Signaling Pathways and Interactions
1.05
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