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3IKD

Structure-Based Design of Novel PIN1 Inhibitors (I)

Summary for 3IKD
Entry DOI10.2210/pdb3ikd/pdb
Related3I6C 3IK8 3IKG
DescriptorPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1, (2R)-2-[(1-benzothiophen-2-ylcarbonyl)amino]-3-phenylpropyl phosphate (3 entities in total)
Functional Keywordssbdd, ppiase, cell cycle, isomerase, small molecule, nucleus, phosphoprotein, rotamase
Biological sourceHomo sapiens (human)
Cellular locationNucleus: Q13526
Total number of polymer chains2
Total formula weight28103.12
Authors
Matthews, D.,Greasley, S.,Ferre, R.,Parge, H. (deposition date: 2009-08-05, release date: 2009-09-22, Last modification date: 2024-02-21)
Primary citationGuo, 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: 19729306
DOI: 10.1016/j.bmcl.2009.08.034
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

226707

數據於2024-10-30公開中

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