In:
Acta Crystallographica Section F Structural Biology Communications, International Union of Crystallography (IUCr), Vol. 72, No. 11 ( 2016-11-01), p. 840-845
Abstract:
Crystals of phosphorylated JAK1 kinase domain were initially generated in complex with nucleotide (ADP) and magnesium. The tightly bound Mg 2+ -ADP at the ATP-binding site proved recalcitrant to ligand displacement. Addition of a molar excess of EDTA helped to dislodge the divalent metal ion, promoting the release of ADP and allowing facile exchange with ATP-competitive small-molecule ligands. Many kinases require the presence of a stabilizing ligand in the ATP site for crystallization. This procedure could be useful for developing co-crystallization systems with an exchangeable ligand to enable structure-based drug design of other protein kinases.
Type of Medium:
Online Resource
ISSN:
2053-230X
DOI:
10.1107/S2053230X16016356
Language:
Unknown
Publisher:
International Union of Crystallography (IUCr)
Publication Date:
2016
detail.hit.zdb_id:
2175956-X
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