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PDBsum entry 1phr

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Phosphotyrosine protein phosphatase PDB id
1phr
Jmol
Contents
Protein chain
154 a.a.
Ligands
SO4
Waters ×70

References listed in PDB file
Key reference
Title The crystal structure of a low-Molecular-Weight phosphotyrosine protein phosphatase.
Authors X.D.Su, N.Taddei, M.Stefani, G.Ramponi, P.Nordlund.
Ref. Nature, 1994, 370, 575-578.
PubMed id 8052313
Abstract
Protein tyrosine phosphorylation and dephosphorylation are central reactions for control of cellular division, differentiation and development. Here we describe the crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase (PTPase), a cytosolic phosphatase present in many mammalian cells. The enzyme catalyses the dephosphorylation of phosphotyrosine-containing substrates, and overexpression of the protein in normal and transformed cells inhibits cell proliferation. The structure of the low-molecular-weight PTPase reveals an alpha/beta protein containing a phosphate-binding loop motif at the amino end of helix alpha 1. This motif includes the essential active-site residues Cys 12 and Arg 18 and bears striking similarities to the active-site motif recently described in the structure of human PTP1B. The structure of the low-molecular-weight PTPase supports a reaction mechanism involving the conserved Cys 12 as an attacking nucleophile in an in-line associative mechanism. The structure also suggests a catalytic role for Asp 129 in the reaction cycle.
Secondary reference #1
Title Crystallisation of a low molecular weight phosphotyrosine protein phosphatase from bovine liver.
Authors X.D.Su, E.G.Agango, N.Taddei, M.Bucciantini, M.Stefani, G.Ramponi, P.Nordlund.
Ref. FEBS Lett, 1994, 343, 107-108. [DOI no: 10.1016/0014-5793(94)80299-8]
PubMed id 8168614
Full text Abstract
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