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Syk 624

Maninder Kaur, Malkeet Singh Bahia, Om Silakari
In the present study, 3D-QSAR analysis was performed utilizing docking based alignment of [1,6]-naphthyridine derivatives as Syk enzyme inhibitors. The role of the water molecules was explored for the docking based alignment that revealed two conserved water molecules important for proper orientation and alignment of naphthyridine inhibitors in the active site of Syk enzyme. The QSAR model was selected having highest value of Q(2) (0.624) and Pearson-r (0.862). The selected model also displayed the highest values of R(2) (0...
October 22, 2012: Journal of Chemical Information and Modeling
Rodrigo O de Castro, Juan Zhang, Maria C Jamur, Constance Oliver, Reuben P Siraganian
The Syk tyrosine kinase family plays an essential role in immunoreceptor tyrosine-based activation motif (ITAM) signaling. The binding of Syk to tyrosine-phosphorylated ITAM subunits of immunoreceptors, such as FcepsilonRI on mast cells, results in a conformational change, with an increase of enzymatic activity of Syk. This conformational change exposes the COOH-terminal tail of Syk, which has three conserved Tyr residues (Tyr-623, Tyr-624, and Tyr-625 of rat Syk). To understand the role of these residues in signaling, wild-type and mutant Syk with these three Tyr mutated to Phe was expressed in Syk-deficient mast cells...
August 20, 2010: Journal of Biological Chemistry
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