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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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Contents |
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* Residue conservation analysis
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PDB id:
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Signaling protein
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Title:
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Crystal structure of ph domain of bruton's tyrosine kinase
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Structure:
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Tyrosine-protein kinase btk. Chain: a, b, c, d. Fragment: ph domain. Synonym: bruton tyrosine kinase, agammaglobulinaemia tyrosine kinase, atk, b cell progenitor kinase, bpk. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_cell_line: sf9.
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Resolution:
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2.58Å
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R-factor:
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0.242
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R-free:
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0.300
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Authors:
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K.Murayama,M.Kato-Murayama,C.Mishima,M.Shirouzu,S.Yokoyama,Riken Structural Genomics/proteomics Initiative (Rsgi)
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Key ref:
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K.Murayama
et al.
(2008).
Crystal structure of the Bruton's tyrosine kinase PH domain with phosphatidylinositol.
Biochem Biophys Res Commun,
377,
23-28.
PubMed id:
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Date:
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07-May-07
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Release date:
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13-May-08
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PROCHECK
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Headers
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References
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Q06187
(BTK_HUMAN) -
Tyrosine-protein kinase BTK from Homo sapiens
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Seq:
Struc:
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659 a.a.
158 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Enzyme class:
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E.C.2.7.10.2
- non-specific protein-tyrosine kinase.
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Reaction:
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L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H+
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L-tyrosyl-[protein]
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+
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ATP
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=
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O-phospho-L-tyrosyl-[protein]
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+
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ADP
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Biochem Biophys Res Commun
377:23-28
(2008)
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PubMed id:
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Crystal structure of the Bruton's tyrosine kinase PH domain with phosphatidylinositol.
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K.Murayama,
M.Kato-Murayama,
C.Mishima,
R.Akasaka,
M.Shirouzu,
Y.Fukui,
S.Yokoyama.
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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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Links
