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PDBsum entry 5ftt
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Signaling protein
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PDB id
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5ftt
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Contents |
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262 a.a.
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326 a.a.
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365 a.a.
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263 a.a.
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PDB id:
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| Name: |
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Signaling protein
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Title:
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Octameric complex of latrophilin 3 (lec, olf) , unc5d (ig, ig2, tsp1) and flrt2 (lrr)
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Structure:
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Netrin receptor unc5d. Chain: a, e. Fragment: ig1 ig2 tsp1. Synonym: protein unc-5 homolog d, unc5d. Engineered: yes. Leucine-rich repeat transmembrane protein flrt2. Chain: b, f. Fragment: leucine-rich repeat domain. Synonym: fibronectin leucine rich transmembrane protein 2, flrt2.
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Source:
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Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek293. Mus musculus. House mouse. Organism_taxid: 10090.
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Resolution:
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3.40Å
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R-factor:
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0.226
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R-free:
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0.245
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Authors:
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V.A.Jackson,S.Mehmood,M.Chavent,P.Roversi,M.Carrasquero,D.Del Toro, G.Seyit-Bremer,F.M.Ranaivoson,D.Comoletti,M.S.P.Sansom,C.V.Robinson, R.Klein,E.Seiradake
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Key ref:
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V.A.Jackson
et al.
(2016).
Super-complexes of adhesion GPCRs and neural guidance receptors.
Nat Commun,
7,
11184.
PubMed id:
DOI:
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Date:
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15-Jan-16
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Release date:
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04-May-16
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PROCHECK
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Headers
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References
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F1LW30
(UNC5D_RAT) -
Netrin receptor UNC5D from Rattus norvegicus
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Seq:
Struc:
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956 a.a.
262 a.a.
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Q8BLU0
(FLRT2_MOUSE) -
Leucine-rich repeat transmembrane protein FLRT2 from Mus musculus
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Seq:
Struc:
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660 a.a.
326 a.a.
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DOI no:
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Nat Commun
7:11184
(2016)
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PubMed id:
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Super-complexes of adhesion GPCRs and neural guidance receptors.
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V.A.Jackson,
S.Mehmood,
M.Chavent,
P.Roversi,
M.Carrasquero,
D.Del Toro,
G.Seyit-Bremer,
F.M.Ranaivoson,
D.Comoletti,
M.S.Sansom,
C.V.Robinson,
R.Klein,
E.Seiradake.
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ABSTRACT
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Latrophilin adhesion-GPCRs (Lphn1-3 or ADGRL1-3) and Unc5 cell guidance
receptors (Unc5A-D) interact with FLRT proteins (FLRT1-3), thereby promoting
cell adhesion and repulsion, respectively. How the three proteins interact and
function simultaneously is poorly understood. We show that Unc5D interacts with
FLRT2 in cis, controlling cell adhesion in response to externally presented
Lphn3. The ectodomains of the three proteins bind cooperatively. Crystal
structures of the ternary complex formed by the extracellular domains reveal
that Lphn3 dimerizes when bound to FLRT2:Unc5, resulting in a stoichiometry of
1:1:2 (FLRT2:Unc5D:Lphn3). This 1:1:2 complex further dimerizes to form a larger
'super-complex' (2:2:4), using a previously undescribed binding motif in the
Unc5D TSP1 domain. Molecular dynamics simulations, point-directed mutagenesis
and mass spectrometry demonstrate the stability and molecular properties of
these complexes. Our data exemplify how receptors increase their functional
repertoire by forming different context-dependent higher-order complexes.
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