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1fpr
From Proteopedia
| 1fpr, resolution 2.50Å () | |||||||||
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| Non-Standard Residues: | |||||||||
| Activity: | Protein-tyrosine-phosphatase, with EC number 3.1.3.48 | ||||||||
| Domains: | PTPc, PTPc | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN THE CATALYTIC DOMAIN OF SHP-1 AND AN IN VITRO PEPTIDE SUBSTRATE PY469 DERIVED FROM SHPS-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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1FPR is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- 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
Page seeded by OCA on Tue Feb 17 18:34:25 2009
