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PDBsum entry 1mai
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Signal transduction protein
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PDB id
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1mai
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References listed in PDB file
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Key reference
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Title
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Structure of the high affinity complex of inositol trisphosphate with a phospholipase c pleckstrin homology domain.
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Authors
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K.M.Ferguson,
M.A.Lemmon,
J.Schlessinger,
P.B.Sigler.
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Ref.
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Cell, 1995,
83,
1037-1046.
[DOI no: ]
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PubMed id
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Abstract
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The X-ray crystal structure of the high affinity complex between the pleckstrin
homology (PH) domain from rat phospholipase C-delta 1 (PLC-delta 1) and
inositol-(1,4,5)-trisphosphate (Ins(1,4,5)P3) has been refined to 1.9 A
resolution. The domain fold is similar to others of known structure.
Ins(1,4,5)P3 binds on the positively charged face of the electrostatically
polarized domain, interacting predominantly with the beta 1/beta 2 and beta
3/beta 4 loops. The 4- and 5-phosphate groups of Ins(1,4,5)P3 interact much more
extensively than the 1-phosphate. Two amino acids in the PLC-delta 1 PH domain
that contact Ins(1,4,5)P3 have counterparts in the Bruton's tyrosine kinase
(Btk) PH domain, where mutational changes cause inherited agammaglobulinemia,
suggesting a mechanism for loss of function in Btk mutants. Using electrostatics
and varying levels of head-group specificity, PH domains may localize and orient
signaling proteins, providing a general membrane targeting and regulatory
function.
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