Literature summary for 2.7.10.2 extracted from

Levinson, N.; Boxer, S.
Structural and spectroscopic analysis of the kinase inhibitor bosutinib and an isomer of bosutinib binding to the Abl tyrosine kinase domain (2012), PLoS ONE, 7, e29828.

Search for more literature for 2.7.10.2

Application

Application	Comment	Organism
analysis	the fluorescence properties of bosutinib and related compounds allow inhibitor binding to be measured quantitatively, and the infrared absorption of the nitrile group reveals a different electrostatic environment in the conserved ATP-binding sites of Abl and Src kinases	Homo sapiens

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
inhibitor bosutinib bound to the kinase domain of isoform Abl, to 2.4 A resolution. Two distinct chemical compounds are currently being sold under the name bosutinib, spectroscopic and structural characterizations of both Structure reveals that similar inhibitors that lack a nitrile moiety could be effective against the common T315I mutant	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
bosutinib	two distinct chemical compounds are currently being sold under the name bosutinib, spectroscopic and structural characterizations of both	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P00519	ABL1	-

Synonyms

Synonyms	Comment	Organism
Abl	-	Homo sapiens

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Release 2023.1 (January 2023)