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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Structural basis for substrate specificity of protein-tyrosine phosphatase SHP-1.

The substrate specificity of the catalytic domain of SHP-1, an important regulator in the proliferation and development of hematopoietic cells, is critical for understanding the physiological functions of SHP-1. Here we report the crystal structures of the catalytic domain of SHP-1 complexed with two peptide substrates derived from SIRPalpha, a member of the signal-regulatory proteins. We show that the variable beta5-loop-beta6 motif confers SHP-1 substrate specificity at the P-4 and further N-terminal subpockets. We also observe a novel residue shift at P-2, the highly conserved subpocket in protein- tyrosine phosphatases. Our observations provide new insight into the substrate specificity of SHP-1.[1]

References

  1. Structural basis for substrate specificity of protein-tyrosine phosphatase SHP-1. Yang, J., Cheng, Z., Niu, T., Liang, X., Zhao, Z.J., Zhou, G.W. J. Biol. Chem. (2000) [Pubmed]
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