FIIN-2

Description	in vitro: FIIN-2 also moderately inhibits EGFR, with an IC50 of 204 nM. The Cys491 of FGFR2 is the primary labeled site for FIIN-2 binding. FIIN-2 is the first class of inhibitors that can potently inhibit the proliferation of cells dependent upon the gatekeeper mutants of FGFR1 or FGFR2. The co-crystal structure of FGFR4 with FIIN-2 was reported, which unexpectedly exhibits a "DFG-out" covalent binding mode. FIIN-2 maintains the pyrimido[4,5-d] pyrimidinone core of FIIN-1 but removes the two chlorine atoms, which are crucial for FIIN-1's potency against FGFR. FIIN-2 maintains the ability to form a covalent bond with the P-loop cysteine but alter the selectivity profile versus other kinases. Compared with FIIN-1, FIIN-2 displays strong binding to FGFRs and exhibited good overall kinase selectivity. FIIN-2 exhibits much less affinity for EGFR, but FIIN-3 potently bound to WT EGFR and to a subset of EGFR mutants. FIIN-2 inhibits proliferation of FGFR1-4 Ba/F3 cells with EC50s in the nano
Pathways	Angiogenesis/Protein Tyrosine Kinase
Targets	FGFR

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