4LKL
Crystal structure of Plk1 Polo-box domain in complex with PL-55
Summary for 4LKL
| Entry DOI | 10.2210/pdb4lkl/pdb |
| Related | 4LKM |
| Related PRD ID | PRD_001156 |
| Descriptor | Serine/threonine-protein kinase PLK1, PL-55, ADAMANTANE, ... (4 entities in total) |
| Functional Keywords | polo-box domain, transferase-transferase inhibitor complex, transferase/transferase inhibitor |
| Biological source | Homo sapiens (human) More |
| Cellular location | Nucleus: P53350 |
| Total number of polymer chains | 2 |
| Total formula weight | 26624.45 |
| Authors | Lee, W.C.,Song, J.H.,Kim, H.Y. (deposition date: 2013-07-08, release date: 2013-12-11, Last modification date: 2023-11-08) |
| Primary citation | Murugan, R.N.,Ahn, M.,Lee, W.C.,Kim, H.Y.,Song, J.H.,Cheong, C.,Hwang, E.,Seo, J.H.,Shin, S.Y.,Choi, S.H.,Park, J.E.,Bang, J.K. Exploring the binding nature of pyrrolidine pocket-dependent interactions in the polo-box domain of polo-like kinase 1 Plos One, 8:e80043-e80043, 2013 Cited by PubMed Abstract: Over the years, a great deal of effort has been focused on the design and synthesis of potent, linear peptide inhibitors targeting the polo-like kinase 1 (Plk1), which is critically involved in multiple mitotic processes and has been established as an adverse prognostic marker for tumor patients. Plk1 localizes to its intracellular anchoring sites via its polo-box domain, and inhibiting the Plk1 polo-box domain has been considered as an approach to circumvent the specificity problems associated with inhibiting the conserved adenosine triphosphate-binding pocket. The polo-box domain consists of two different binding regions, such as the unique, broader pyrrolidine-binding pocket and the conserved, narrow, Tyr-rich hydrophobic channel, among the three Plk polo-box domains (Plks 1-3), respectively. Therefore, the studies that provide insights into the binding nature of the unique, broader pyrrolidine-binding pocket might lead to the development of selective Plk1-inhibitory compounds. PubMed: 24223211DOI: 10.1371/journal.pone.0080043 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.58 Å) |
Structure validation
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