Structural basis of human ABCC4 recognition of cAMP and ligand recognition flexibility

These results suggest that hABCC4 can bind cAMP and exhibits varying degrees of flexibility when binding with different substrates, including cAMP. These findings expand our understanding of the structural biology of ABCC4.

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Publication Details

Journal
Cell & Bioscience
Published
2025-03-27
DOI
https://doi.org/10.1186/s13578-025-01377-y
Citations
3
Primary Topic
Drug Transport and Resistance Mechanisms
Type
article
Field-Weighted Citation Impact
3.14

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article

Structural basis of human ABCC4 recognition of cAMP and ligand recognition flexibility

Weiming Tian, Xin Wen, Kaixue Si, Anqi Zhang et al.
3 citations
Cell & Bioscience
Drug Transport and Resistance Mechanisms
3.14
article

Structural basis of human ABCC4 recognition of cAMP and ligand recognition flexibility

Weiming Tian, Xin Wen, Kaixue Si, Anqi Zhang, Changyou Guo, Minghui Li, Dantong Zhu
article en
3 citations

Abstract

These results suggest that hABCC4 can bind cAMP and exhibits varying degrees of flexibility when binding with different substrates, including cAMP. These findings expand our understanding of the structural biology of ABCC4.

Cell & BioscienceVol. 15(1)
Harbin Institute of Technology (CN)
Harbin Institute of Technology
Good health and well-being
Openalex Percentile: Top 9%
Drug Transport and Resistance Mechanisms
3.14
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