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PDBsum entry 6n8s
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Lipid binding protein
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PDB id
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6n8s
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PDB id:
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| Name: |
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Lipid binding protein
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Title:
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Crystal structure of the human cell polarity protein lethal giant larvae 2 (lgl2). Apkc phosphorylated, crystal form 3.
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Structure:
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Lethal(2) giant larvae protein homolog 2. Chain: a, d. Synonym: hgl. Engineered: yes. Other_details: human lgl2(13-978) apkc phosphorylated at s641, s645, s649, s653, s660, s663 and s680
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: llgl2. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_cell_line: sf9
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Resolution:
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3.90Å
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R-factor:
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0.256
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R-free:
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0.298
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Authors:
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L.Almagor,W.I.Weis
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Key ref:
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L.Almagor
et al.
(2019).
Structural insights into the aPKC regulatory switch mechanism of the human cell polarity protein lethal giant larvae 2.
Proc Natl Acad Sci U S A,
116,
10804-10812.
PubMed id:
DOI:
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Date:
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30-Nov-18
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Release date:
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08-May-19
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PROCHECK
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Headers
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References
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Q6P1M3
(L2GL2_HUMAN) -
LLGL scribble cell polarity complex component 2 from Homo sapiens
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Seq:
Struc:
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1020 a.a.
834 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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DOI no:
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Proc Natl Acad Sci U S A
116:10804-10812
(2019)
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PubMed id:
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Structural insights into the aPKC regulatory switch mechanism of the human cell polarity protein lethal giant larvae 2.
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L.Almagor,
I.S.Ufimtsev,
A.Ayer,
J.Li,
W.I.Weis.
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ABSTRACT
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Metazoan cell polarity is controlled by a set of highly conserved proteins.
Lethal giant larvae (Lgl) functions in apical-basal polarity through
phosphorylation-dependent interactions with several other proteins as well as
the plasma membrane. Phosphorylation of Lgl by atypical protein kinase C (aPKC),
a component of the partitioning-defective (Par) complex in epithelial cells,
excludes Lgl from the apical membrane, a crucial step in the establishment of
epithelial cell polarity. We present the crystal structures of human Lgl2 in
both its unphosphorylated and aPKC-phosphorylated states. Lgl2 adopts a double
β-propeller structure that is unchanged by aPKC phosphorylation of an
unstructured loop in its second β-propeller, ruling out models of
phosphorylation-dependent conformational change. We demonstrate that
phosphorylation controls the direct binding of purified Lgl2 to negative
phospholipids in vitro. We also show that a coil-helix transition of this region
that is promoted by phosphatidylinositol 4,5-bisphosphate (PIP2) is
also phosphorylation-dependent, implying a highly effective phosphorylative
switch for membrane association.
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