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PDBsum entry 1pls
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Phosphorylation
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PDB id
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1pls
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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 pleckstrin-Homology domain.
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Authors
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H.S.Yoon,
P.J.Hajduk,
A.M.Petros,
E.T.Olejniczak,
R.P.Meadows,
S.W.Fesik.
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Ref.
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Nature, 1994,
369,
672-675.
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PubMed id
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Abstract
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Pleckstrin, the major protein kinase C substrate of platelets, contains domains
of about 100 amino acids at the amino and carboxy termini that have been found
in a number of proteins, including serine/threonine kinases, GTPase-activating
proteins, phospholipases and cytoskeletal proteins. These conserved sequences,
termed pleckstrin-homology (PH) domains, are thought to be involved in signal
transduction. But the details of the function and binding partners of the PH
domains have not been characterized. Here we report the solution structure of
the N-terminal pleckstrin-homology domain of pleckstrin determined using
heteronuclear three-dimensional nuclear magnetic resonance spectroscopy. The
structure consists of an up-and-down beta-barrel of seven antiparallel
beta-strands and a C-terminal amphiphilic alpha-helix that caps one end of the
barrel. The overall topology of the domain is similar to that of the
retinol-binding protein family of structures.
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Secondary reference #1
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Title
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Pleckstrin homology domains bind to phosphatidylinositol-4,5-Bisphosphate.
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Authors
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J.E.Harlan,
P.J.Hajduk,
H.S.Yoon,
S.W.Fesik.
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Ref.
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Nature, 1994,
371,
168-170.
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PubMed id
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