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PDBsum entry 2z0p
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Signaling protein
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PDB id
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2z0p
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the bruton'S tyrosine kinase ph domain with phosphatidylinositol.
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Authors
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K.Murayama,
M.Kato-Murayama,
C.Mishima,
R.Akasaka,
M.Shirouzu,
Y.Fukui,
S.Yokoyama.
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Ref.
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Biochem Biophys Res Commun, 2008,
377,
23-28.
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PubMed id
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Abstract
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Bruton's tyrosine kinase (Btk) of the Tec family possesses a Pleckstrin homology
(PH) domain, which is responsible for plasma membrane targeting. In this study,
the crystal structure of the Btk PH domain in complex with
dibutylyl-phosphatidylinositol-3,4,5-triphosphate was determined. The structure
revealed that the Btk PH domain forms a homodimer and that each molecule binds
phosphatidylinositol in the binding pocket. The side chain of Lys18 within a
Btk-specific insertion in the beta1-beta2 loop is able to form a hydrogen bond
with the diacylglycerol moiety of phosphatidylinositol. The other Btk-specific
insertion in the beta5-beta6 loop constitutes the dimerization interface. Thus,
the modes of phosphatidylinositol recognition and Btk PH domain dimerization are
distinct from those of other PH domains.
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