Figure 1
Figure 1. Map of all the amino acid substitutions in the Bcr-Abl KD identified in clinical samples from patients reported to be resistant to imatinib in published papers. Key structural motifs within the KD are indicated. P-loop indicates phosphate binding loop; SH2 contact and SH3 contact, contact regions with SH2 and SH3 domain-containing proteins; and A-loop, activation loop. Star indicates amino acid position reported to be directly involved in imatinib binding via hydrogen bonds or van der Waals interactions.7 K247R and Y320C are in italic because they have been reported to be single nucleotide polymorphisms. Numbering of residues is according to Abl Ia isoform. Data were collated from 27 studies published between 2001 and 2009.1–6,14,16,17,28,35,51–53,61,62,72,82–91

Map of all the amino acid substitutions in the Bcr-Abl KD identified in clinical samples from patients reported to be resistant to imatinib in published papers. Key structural motifs within the KD are indicated. P-loop indicates phosphate binding loop; SH2 contact and SH3 contact, contact regions with SH2 and SH3 domain-containing proteins; and A-loop, activation loop. Star indicates amino acid position reported to be directly involved in imatinib binding via hydrogen bonds or van der Waals interactions. K247R and Y320C are in italic because they have been reported to be single nucleotide polymorphisms. Numbering of residues is according to Abl Ia isoform. Data were collated from 27 studies published between 2001 and 2009.1-6,14,16,17,28,35,51-53,61,62,72,82-91 

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