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PDBsum entry 5c6r
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Signaling protein
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PDB id
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5c6r
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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 asap1
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Structure:
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Arf-gap. Chain: a, b. Fragment: ph domain. Synonym: 130 kda phosphatidylinositol 4,5-bisphosphate-dependent arf1 gtpase-activating protein,adp-ribosylation factor-directed gtpase- activating protein 1,arf gtpase-activating protein 1,development and differentiation-enhancing factor 1,differentiation-enhancing factor 1,pip2-dependent arf1 gap. Engineered: yes
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Source:
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Mus musculus. Mouse. Organism_taxid: 10090. Gene: asap1, ddef1, kiaa1249, shag1. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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1.80Å
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R-factor:
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0.211
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R-free:
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0.260
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Authors:
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D.Xia,W.K.Tang
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Key ref:
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X.Jian
et al.
(2015).
Molecular Basis for Cooperative Binding of Anionic Phospholipids to the PH Domain of the Arf GAP ASAP1.
Structure,
23,
1977-1988.
PubMed id:
DOI:
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Date:
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23-Jun-15
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Release date:
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07-Oct-15
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PROCHECK
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Headers
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References
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Q9QWY8
(ASAP1_MOUSE) -
Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 from Mus musculus
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Seq:
Struc:
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1147 a.a.
110 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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DOI no:
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Structure
23:1977-1988
(2015)
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PubMed id:
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Molecular Basis for Cooperative Binding of Anionic Phospholipids to the PH Domain of the Arf GAP ASAP1.
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X.Jian,
W.K.Tang,
P.Zhai,
N.S.Roy,
R.Luo,
J.M.Gruschus,
M.E.Yohe,
P.W.Chen,
Y.Li,
R.A.Byrd,
D.Xia,
P.A.Randazzo.
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ABSTRACT
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We have defined the molecular basis for association of the PH domain of the Arf
GAP ASAP1 with phospholipid bilayers. Structures of the unliganded and dibutyryl
PtdIns(4,5)P2-bound PH domain were solved. PtdIns(4,5)P2 made contact with both
a canonical site (C site) and an atypical site (A site). We hypothesized
cooperative binding of PtdIns(4,5)P2 to the C site and a nonspecific anionic
phospholipid to the A site. PtdIns(4,5)P2 dependence of binding to large
unilamellar vesicles and GAP activity was sigmoidal, consistent with cooperative
sites. In contrast, PtdIns(4,5)P2 binding to the PH domain of PLC δ1 was
hyperbolic. Mutation of amino acids in either the C or A site resulted in
decreased PtdIns(4,5)P2-dependent binding to vesicles and decreased GAP
activity. The results support the idea of cooperative phospholipid binding to
the C and A sites of the PH domain of ASAP1. We propose that the mechanism
underlies rapid switching between active and inactive ASAP1.
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Links
