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|1phr, resolution 2.10Å ()|
THE CRYSTAL STRUCTURE OF A LOW MOLECULAR PHOSPHOTYROSINE PROTEIN PHOSPHATASE
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.
The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase., Su XD, Taddei N, Stefani M, Ramponi G, Nordlund P, Nature. 1994 Aug 18;370(6490):575-8. PMID:8052313
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
- Su XD, Taddei N, Stefani M, Ramponi G, Nordlund P. The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase. Nature. 1994 Aug 18;370(6490):575-8. PMID:8052313 doi:http://dx.doi.org/10.1038/370575a0
- Thomas A, Bouffioux O, Geeurickx D, Brasseur R. Pex, analytical tools for PDB files. I. GF-Pex: basic file to describe a protein. Proteins. 2001 Apr 1;43(1):28-36. PMID:11170211
- Sandelin E. On hydrophobicity and conformational specificity in proteins. Biophys J. 2004 Jan;86(1 Pt 1):23-30. PMID:14695246 doi:10.1016/S0006-3495(04)74080-1