Structural basis for the auto-inhibition of c-Abl tyrosine kinase

Structural basis for the autoinhibition of c-Abl tyrosine kinase

A myristoyl/phosphotyrosine switch regulates c-Abl

N-terminal 531 residues (MYR-SH3-SH2-Kinase domain)

0.8 M ammonium tartrate , pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K

C-ABL KINASE DOMAIN IN COMPLEX WITH A MYRISTOYLATED PEPTIDE

C-ABL SH3-SH2-KINASE DOMAINS IN COMPLEX WITH MYRISTIC ACID

SEQUENCE
The bound myristoyl group is from the naturally
occurring N-terminal myristoyl modification that
is connected to the SH3 domain of the protein chain A
by 79 residues that could not be modeled. An O
atom has been intentionally omitted from MYR since
the O atom is not chemically present in a myristoyl
group that is attached to the protein.

The structure was refined by superimposing the refined high resolution structure of c-Abl (pdb entry 1OPK) on the molecular replacement solution and optimizing positions of individual domains by rigid-body refinement. Following this, only overall domain B-factors were applied to molecule B, whereas individual B-factors were refined for molecule A.