5UT4

JAK2 JH2 in complex with NVP-BSK805

Summary for 5UT4

• Entry DOI: 10.2210/pdb5ut4/pdb
• Related: 5USY 5USZ 5UT0 5UT1 5UT2 5UT3 5UT5 5UT6
• Descriptor: Tyrosine-protein kinase JAK2, 8-[3,5-difluoro-4-(morpholin-4-ylmethyl)phenyl]-2-(1-piperidin-4-yl-1H-pyrazol-4-yl)quinoxaline, GLYCEROL, ... (5 entities in total)
• Functional Keywords: pseudokinase domain, transferase-transferase inhibitor complex, transferase/transferase inhibitor
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 33873.83

Authors

Puleo, D.E.,Schlessinger, J. (deposition date: 2017-02-14, release date: 2017-06-07, Last modification date: 2023-10-04)

Primary citation

Newton, A.S.,Deiana, L.,Puleo, D.E.,Cisneros, J.A.,Cutrona, K.J.,Schlessinger, J.,Jorgensen, W.L.
JAK2 JH2 Fluorescence Polarization Assay and Crystal Structures for Complexes with Three Small Molecules.
ACS Med Chem Lett, 8:614-617, 2017

PubMed Abstract: A competitive fluorescence polarization (FP) assay is reported for determining binding affinities of probe molecules with the pseudokinase JAK2 JH2 allosteric site. The syntheses of the fluorescent and used in the assay are reported as well as results for 10 compounds, including JNJ7706621, NVP-BSK805, and filgotinib (GLPG0634). X-ray crystal structures of JAK2 JH2 in complex with NVP-BSK805, filgotinib, and diaminopyrimidine elucidate the binding poses.

PubMed: 28626520
DOI: 10.1021/acsmedchemlett.7b00154

Experimental method

X-RAY DIFFRACTION (2 Å)