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Solution structure of a low molecular weight protein tyrosine phosphatase.

Logan TM, Zhou MM, Nettesheim DG, Meadows RP, Van Etten RL, Fesik SW
Biochemistry 33 11087-96 (1994)
Cited: 24 times
EuropePMC logo PMID: 7727361

Abstract

Protein tyrosine phosphatases (PTPs) are important enzymes involved in signal transduction, cell cycle regulation, and the control of differentiation. Despite the importance of this class of enzymes in the control of critical cell processes, very little structural information is available for this family of proteins. In this paper, we present the first solution structure of a protein tyrosine phosphatase. This protein is a low molecular weight cytosolic PTP that was initially isolated from bovine heart. The structure that was determined from 1747 NMR-derived restraints consists of a central four-stranded parallel beta-sheet surrounded by four alpha-helices and a short 3(10) helix. The phosphate binding site, identified by chemical shift changes upon the addition of the competitive inhibitors phosphate and vanadate, is in a loop region connecting the C-terminal end of the first beta-strand with the first alpha-helix. Residues in the second, fourth, and fifth alpha-helices and in some of the loop regions connecting the elements of regular secondary structure also contribute to the binding site. The structure determined here is consistent with previous mutagenesis and chemical modification studies conducted on this protein.

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  2. Diabetes reversal by inhibition of the low-molecular-weight tyrosine phosphatase. Stanford SM, Aleshin AE, Zhang V, Ardecky RJ, Hedrick MP, Zou J, Ganji SR, Bliss MR, Yamamoto F, Bobkov AA, Kiselar J, Liu Y, Cadwell GW, Khare S, Yu J, Barquilla A, Chung TDY, Mustelin T, Schenk S, Bankston LA, Liddington RC, Pinkerton AB, Bottini N. Nat Chem Biol 13 624-632 (2017)
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  14. Mechanism of substrate dephosphorylation in low Mr protein tyrosine phosphatase. Kolmodin K, Nordlund P, Aqvist J. Proteins 36 370-379 (1999)
  15. Solution structure of the low-molecular-weight protein tyrosine phosphatase from Tritrichomonas foetus reveals a flexible phosphate binding loop. Gustafson CL, Stauffacher CV, Hallenga K, Van Etten RL. Protein Sci 14 2515-2525 (2005)
  16. Letter 1H, 15N, and 13C resonance assignments of low molecular weight human cytoplasmic protein tyrosine phosphatase-A (HCPTP-A). Rastogi VK, Diven CF, Seabrook GM, Genbauffe FS, Bechard RT, Fandl JP, Peters KG. J Biomol NMR 23 251-252 (2002)
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Related citations provided by authors (1)

  1. Backbone 1H, 13C, and 15N Assignments and Secondary Structure of Bovine Low-Molecular-Weight Phosphotyrosyl Protein Phosphatase. Zhou M-M, Logan TM, Theriault Y, Van Etten RL, Fesik SW Biochemistry 33 5221- (1994)

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