9KRM
Cryo-EM structure of human ABCC4 (MTX-bound)
9KRM の概要
| エントリーDOI | 10.2210/pdb9krm/pdb |
| EMDBエントリー | 62533 |
| 分子名称 | ATP-binding cassette sub-family C member 4, METHOTREXATE (2 entities in total) |
| 機能のキーワード | abc-type transporter activity, atp hydrolysis activity, atpase-coupled transmembrane transporter activity, atp binding, transport protein., transport protein |
| 由来する生物種 | Homo sapiens (human) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 150148.36 |
| 構造登録者 | |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3 Å) |
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