9KRM
Cryo-EM structure of human ABCC4 (MTX-bound)
Summary for 9KRM
| Entry DOI | 10.2210/pdb9krm/pdb |
| EMDB information | 62533 |
| Descriptor | ATP-binding cassette sub-family C member 4, METHOTREXATE (2 entities in total) |
| Functional Keywords | abc-type transporter activity, atp hydrolysis activity, atpase-coupled transmembrane transporter activity, atp binding, transport protein., transport protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 150148.36 |
| Authors | |
| Primary citation | Wen, X.,Si, K.,Zhu, D.,Zhang, A.,Guo, C.,Li, M.,Tian, W. Structural basis of human ABCC4 recognition of cAMP and ligand recognition flexibility. Cell Biosci, 15:39-39, 2025 Cited by PubMed Abstract: ABCC4 (ATP-binding cassette sub-family C member 4) is a transporter protein that is primarily localized to the plasma membrane, and its efflux activity is associated with the progression of various cancers and the development of drug resistance. Cyclic adenosine monophosphate (cAMP) is an important biomolecule that is considered a transport substrate of ABCC4. However, there is currently no direct structural understanding of how ABCC4 binds cAMP, and the mechanisms by which it recognizes a diverse range of substrate ligands remain poorly understood. Some studies have indicated that, under physiological conditions, cAMP does not significantly stimulate the ATPase activity of ABCC4, making the commonly used ATPase activity assays for ABC proteins unsuitable for studying cAMP. PubMed: 40148998DOI: 10.1186/s13578-025-01377-y PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3 Å) |
Structure validation
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