2b3o
From Proteopedia
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Crystal structure of human tyrosine phosphatase SHP-1
Overview
SHP-1 is a cytosolic protein-tyrosine phosphatase that behaves as a, negative regulator in eukaryotic cellular signaling pathways. To, understand its regulatory mechanism, we have determined the crystal, structure of the C-terminal truncated human SHP-1 in the inactive, conformation at 2.8-A resolution and refined the structure to a, crystallographic R-factor of 24.0%. The three-dimensional structure shows, that the ligand-free SHP-1 has an auto-inhibited conformation. Its N-SH2, domain blocks the catalytic domain and keeps the enzyme in the inactive, conformation, which supports that the phosphatase activity of SHP-1 is, primarily regulated by the N-SH2 domain. In addition, the C-SH2 domain of, SHP-1 has a different orientation from and is more flexible than that of, SHP-2, which enables us to propose an enzymatic activation mechanism in, which the C-SH2 domains of SHPs could be involved in searching for, phosphotyrosine activators.
About this Structure
2B3O is a Single protein structure of sequence from Homo sapiens. Active as Protein-tyrosine-phosphatase, with EC number 3.1.3.48 Full crystallographic information is available from OCA.
Reference
Crystal structure of human protein-tyrosine phosphatase SHP-1., Yang J, Liu L, He D, Song X, Liang X, Zhao ZJ, Zhou GW, J Biol Chem. 2003 Feb 21;278(8):6516-20. Epub 2002 Dec 13. PMID:12482860
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