Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
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.
Structural basis for substrate specificity of protein-tyrosine phosphatase SHP-1.,Yang J, Cheng Z, Niu T, Liang X, Zhao ZJ, Zhou GW J Biol Chem. 2000 Feb 11;275(6):4066-71. PMID:10660565[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yang J, Cheng Z, Niu T, Liang X, Zhao ZJ, Zhou GW. Structural basis for substrate specificity of protein-tyrosine phosphatase SHP-1. J Biol Chem. 2000 Feb 11;275(6):4066-71. PMID:10660565
