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PDBsum entry 1bvh
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References listed in PDB file
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Key reference
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Title
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Solution structure of a low molecular weight protein tyrosine phosphatase.
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Authors
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T.M.Logan,
M.M.Zhou,
D.G.Nettesheim,
R.P.Meadows,
R.L.Van etten,
S.W.Fesik.
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Ref.
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Biochemistry, 1994,
33,
11087-11096.
[DOI no: ]
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
perfect match.
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Abstract
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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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Secondary reference #1
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Title
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Backbone 1h, 13c, And 15n assignments and secondary structure of bovine low molecular weight phosphotyrosyl protein phosphatase.
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Authors
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M.M.Zhou,
T.M.Logan,
Y.Thèriault,
R.L.Van etten,
S.W.Fesik.
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Ref.
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Biochemistry, 1994,
33,
5221-5229.
[DOI no: ]
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PubMed id
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