3IK8
Structure-Based Design of Novel PIN1 Inhibitors (I)
Summary for 3IK8
| Entry DOI | 10.2210/pdb3ik8/pdb |
| Related | 3I6C 3IKD 3IKG |
| Descriptor | Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (2 entities in total) |
| Functional Keywords | sbdd, ppiase, cell cycle, isomerase, nucleus, phosphoprotein, rotamase |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: Q13526 |
| Total number of polymer chains | 2 |
| Total formula weight | 27324.39 |
| Authors | Matthews, D.,Greasley, S.,Ferre, R.A.,Parge, H. (deposition date: 2009-08-05, release date: 2009-09-22, Last modification date: 2024-02-21) |
| Primary citation | Guo, C.,Hou, X.,Dong, L.,Dagostino, E.,Greasley, S.,Ferre, R.,Marakovits, J.,Johnson, M.C.,Matthews, D.,Mroczkowski, B.,Parge, H.,Vanarsdale, T.,Popoff, I.,Piraino, J.,Margosiak, S.,Thomson, J.,Los, G.,Murray, B.W. Structure-based design of novel human Pin1 inhibitors (I). Bioorg.Med.Chem.Lett., 19:5613-5616, 2009 Cited by PubMed Abstract: Pin1 is a member of the cis-trans peptidyl-prolyl isomerase family with potential anti-cancer therapeutic value. Here we report structure-based de novo design and optimization of novel Pin1 inhibitors. Without a viable lead from internal screenings, we designed a series of novel Pin1 inhibitors by interrogating and exploring a protein crystal structure of Pin1. The ligand efficiency of the initial concept molecule was optimized with integrated SBDD and parallel chemistry approaches, resulting in a more attractive lead series. PubMed: 19729306DOI: 10.1016/j.bmcl.2009.08.034 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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