1FPR

CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN THE CATALYTIC DOMAIN OF SHP-1 AND AN IN VITRO PEPTIDE SUBSTRATE PY469 DERIVED FROM SHPS-1.

Summary for 1FPR

• Entry DOI: 10.2210/pdb1fpr/pdb
• Descriptor: PROTEIN-TYROSINE PHOSPHATASE 1C, PEPTIDE PY469 (2 entities in total)
• Functional Keywords: protein tyrosine phosphatase, substrate specificity, residue shift, signaling protein
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: P29350
• Total number of polymer chains: 2
• Total formula weight: 33793.93

Authors

Yang, J.,Cheng, Z.,Niu, Z.,Zhao, Z.J.,Zhou, G.W. (deposition date: 2000-08-31, release date: 2001-03-07, Last modification date: 2024-10-16)

Primary citation

Yang, J.,Cheng, Z.,Niu, T.,Liang, X.,Zhao, Z.J.,Zhou, G.W.
Structural basis for substrate specificity of protein-tyrosine phosphatase SHP-1.
J.Biol.Chem., 275:4066-4071, 2000

PubMed Abstract: 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.

PubMed: 10660565
DOI: 10.1074/jbc.275.6.4066

Experimental method

X-RAY DIFFRACTION (2.5 Å)