1BVH

SOLUTION STRUCTURE OF A LOW MOLECULAR WEIGHT PROTEIN TYROSINE PHOSPHATASE

Summary for 1BVH

• Entry DOI: 10.2210/pdb1bvh/pdb
• Descriptor: ACID PHOSPHATASE (1 entity in total)
• Functional Keywords: hydrolase
• Biological source: Bos taurus (cattle)
• Cellular location: Cytoplasm: P11064
• Total number of polymer chains: 1
• Total formula weight: 17946.33

Authors

Logan, T.M.,Zhou, M.-M.,Nettesheim, D.G.,Meadows, R.P.,Van Etten, R.L.,Fesik, S.W. (deposition date: 1994-05-03, release date: 1994-07-31, Last modification date: 2024-05-22)

Primary citation

Logan, T.M.,Zhou, M.M.,Nettesheim, D.G.,Meadows, R.P.,Van Etten, R.L.,Fesik, S.W.
Solution structure of a low molecular weight protein tyrosine phosphatase.
Biochemistry, 33:11087-11096, 1994

PubMed 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.

PubMed: 7727361
DOI: 10.1021/bi00203a005

Experimental method

SOLUTION NMR