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==Overview==
==Overview==
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.
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.


==About this Structure==
==About this Structure==
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[[Category: Niu, Z.]]
[[Category: Niu, Z.]]
[[Category: Yang, J.]]
[[Category: Yang, J.]]
[[Category: Zhao, Z.J.]]
[[Category: Zhao, Z J.]]
[[Category: Zhou, G.W.]]
[[Category: Zhou, G W.]]
[[Category: protein tyrosine phosphatase]]
[[Category: protein tyrosine phosphatase]]
[[Category: residue shift]]
[[Category: residue shift]]
[[Category: substrate specificity]]
[[Category: substrate specificity]]


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