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PDBsum entry 5cmp
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Cell adhesion
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PDB id
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5cmp
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References listed in PDB file
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Key reference
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Title
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Structural basis of latrophilin-Flrt-Unc5 interaction in cell adhesion.
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Authors
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Y.C.Lu,
O.V.Nazarko,
R.Sando,
G.S.Salzman,
T.C.Südhof,
D.Araç.
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Ref.
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Structure, 2015,
23,
1678-1691.
[DOI no: ]
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PubMed id
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Abstract
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Fibronectin leucine-rich repeat transmembrane proteins (FLRTs) are cell-adhesion
molecules with emerging functions in cortical development and synapse formation.
Their extracellular regions interact with latrophilins (LPHNs) to mediate
synapse development, and with Uncoordinated-5 (UNC5)/netrin receptors to control
the migration of neurons in the developing cortex. Here, we present the crystal
structures of FLRT3 in isolation and in complex with LPHN3. The LPHN3/FLRT3
structure reveals that LPHN3 binds to FLRT3 at a site distinct from UNC5.
Structure-based mutations specifically disrupt LPHN3/FLRT3 binding, but do not
disturb their interactions with other proteins or their cell-membrane
localization. Thus, they can be used as molecular tools to dissect the functions
of FLRTs and LPHNs in vivo. Our results suggest that UNC5 and LPHN3 can
simultaneously bind to FLRT3, forming a trimeric complex, and that FLRT3 may
form transsynaptic complexes with both LPHN3 and UNC5. These findings provide
molecular insights for understanding the role of cell-adhesion proteins in
synapse function.
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