7W5O
Crystal structure of ERK2 with an allosteric inhibitor
Summary for 7W5O
| Entry DOI | 10.2210/pdb7w5o/pdb |
| Descriptor | Mitogen-activated protein kinase 1, (2R,3R,4S,5R)-2-(4-AMINO-5-IODO-7H-PYRROLO[2,3-D]PYRIMIDIN-7-YL)-5-(HYDROXYMETHYL)TETRAHYDROFURAN-3,4-DIOL, MALONIC ACID, ... (9 entities in total) |
| Functional Keywords | protein kinase, allosteric inhibitor, activation loop, transferase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 87004.71 |
| Authors | Yoshida, M.,Kinoshita, T. (deposition date: 2021-11-30, release date: 2022-02-23, Last modification date: 2023-11-29) |
| Primary citation | Yoshida, M.,Nagao, H.,Sugiyama, H.,Sawa, M.,Kinoshita, T. Identification of a novel target site for ATP-independent ERK2 inhibitors. Biochem.Biophys.Res.Commun., 593:73-78, 2022 Cited by PubMed Abstract: Extracellular signal-regulated kinase 2 (ERK2) controls vital physiological processes involving proliferation and differentiation and is a drug target molecule for many diseases such as cancers. In silico screening focusing on an allosteric site that plays a crucial role in substrate anchoring conferred an ERK2 inhibitor (compound 1). However, a competitive binding assay indicated that compound 1 did not bind to the allosteric site. Here, the crystal structure of ERK2 in complex with compound 1 revealed a novel binding site. This finding demonstrates the feasibility of developing new types of ERK2 inhibitors. PubMed: 35063772DOI: 10.1016/j.bbrc.2022.01.035 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
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