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PDBsum entry 3zyn
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Cell adhesion
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PDB id
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3zyn
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PDB id:
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| Name: |
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Cell adhesion
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Title:
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Crystal structure of the n-terminal leucine rich repeats of netrin-g ligand-3
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Structure:
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Leucine-rich repeat-containing protein 4b. Chain: a, b. Fragment: n-terminal leucine rich repeats, residues 57-365. Synonym: netrin-g3 ligand, ngl-3. Engineered: yes
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Source:
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Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek293s.
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Resolution:
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3.20Å
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R-factor:
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0.219
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R-free:
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0.268
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Authors:
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E.Seiradake,C.H.Coles,P.V.Perestenko,K.Harlos,R.A.J.Mcilhinney, A.R.Aricescu,E.Y.Jones
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Key ref:
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E.Seiradake
et al.
(2011).
Structural basis for cell surface patterning through NetrinG-NGL interactions.
Embo J,
30,
4479-4488.
PubMed id:
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Date:
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23-Aug-11
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Release date:
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05-Oct-11
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PROCHECK
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Headers
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References
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P0C192
(LRC4B_MOUSE) -
Leucine-rich repeat-containing protein 4B from Mus musculus
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Seq:
Struc:
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709 a.a.
310 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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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Embo J
30:4479-4488
(2011)
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PubMed id:
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Structural basis for cell surface patterning through NetrinG-NGL interactions.
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E.Seiradake,
C.H.Coles,
P.V.Perestenko,
K.Harlos,
R.A.McIlhinney,
A.R.Aricescu,
E.Y.Jones.
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ABSTRACT
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Brain wiring depends on cells making highly localized and selective connections
through surface protein-protein interactions, including those between NetrinGs
and NetrinG ligands (NGLs). The NetrinGs are members of the structurally
uncharacterized netrin family. We present a comprehensive crystallographic
analysis comprising NetrinG1-NGL1 and NetrinG2-NGL2 complexes, unliganded
NetrinG2 and NGL3. Cognate NetrinG-NGL interactions depend on three
specificity-conferring NetrinG loops, clasped tightly by matching NGL surfaces.
We engineered these NGL surfaces to implant custom-made affinities for NetrinG1
and NetrinG2. In a cellular patterning assay, we demonstrate that
NetrinG-binding selectivity can direct the sorting of a mixed population of NGLs
into discrete cell surface subdomains. These results provide a molecular model
for selectivity-based patterning in a neuronal recognition system, dysregulation
of which is associated with severe neuropsychological disorders.
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Links
