Selective mutation in ATP-binding site reduces affinity of drug to the kinase: A possible mechanism of chemo-resistance

Medical Oncology

Volumn 30, Issue 1, 2013, Pages

  Kabir, Nuzhat N ^a   Kazi, Julhash U ^a,b  

^a KN Biomedical Research Institute   (Bangladesh)

^b LUND UNIVERSITY   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHOTRANSFERASE INHIBITOR; PROTEIN KINASE C; RUBOXISTAURIN; ADENOSINE TRIPHOSPHATE;

BINDING AFFINITY; BINDING SITE; DRUG BINDING; DRUG STRUCTURE; ENZYME STRUCTURE; GENE MUTATION; HUMAN; LETTER; MOLECULAR DOCKING; PRIORITY JOURNAL; THERAPY RESISTANCE; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; DRUG RESISTANCE; GENETICS; MOLECULAR GENETICS; MUTATION; PROTEIN TERTIARY STRUCTURE;

ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; BINDING SITES; DRUG RESISTANCE, NEOPLASM; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN KINASE C; PROTEIN STRUCTURE, TERTIARY;

EID: 84880634396     PISSN: 13570560     EISSN: 1559131X     Source Type: Journal    
DOI: 10.1007/s12032-012-0448-9     Document Type: Letter

References (3)

1. Williams AB, Nguyen B, Li L, Brown P, Levis M, Leahy D et al. Mutations of FLT3/ITD confer resistance to multiple tyrosine kinase inhibitors. Leukemia: official journal of the Leukemia Society of America, Leukemia Research Fund, UK. 2012. doi: 10.1038/leu.2012.191.
2. Kazi JU. The mechanism of protein kinase C regulation. Front Biol. 2011;6:328-36.
3. Smith CC, Wang Q, Chin CS, Salerno S, Damon LE, Levis MJ, et al. Validation of ITD mutations in FLT3 as a therapeutic target in human acute myeloid leukaemia. Nature. 2012;485(7397):260-3. doi: 10.1038/nature11016.