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Structural Basis of Latrophilin-FLRT-UNC5 Interaction in Cell Adhesion

Structural Basis of Latrophilin-FLRT-UNC5 Interaction in Cell AdhesionFibronectin 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.

Structure. 2015 Sep 1;23(9):1678-91.
doi: 10.1016/j.str.2015.06.024. Epub 2015 Jul 30.

The Cell Press Group
©2015 Elsevier Ltd. All Rights Reserved.

  Lu YC, Nazarko OV, Sando R 3rd, Salzman GS, Südhof TC, Araç D.

Another SBC Highlight:

EsxB, a secreted protein from Bacillus anthracis forms two distinct helical bundles
A highly stable prefusion RSV F vaccine derived from structural analysis of the fusion mechanism

Respiratory syncytial virus (RSV) causes acute lower respiratory tract infections and is the leading cause of infant hospitalizations. Recently, a promising vaccine antigen based on the RSV fusion protein (RSV F) stabilized in the native prefusion conformation has been described. Here we report alternative strategies to arrest RSV F in the prefusion conformation based on the prevention of hinge movements in the first refolding region and the elimination of proteolytic exposure of the fusion peptide.


Nat Commun. 2015 Sep 3;6:8143.
doi: 10.1038/ncomms9143.

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The on-line SBC Beamtime Request System allows users to view available beamtime on 19-ID and 19-BM, and to submit a request for rapid beamtime allocation.

Beamtime is available to the research community via a peer reviewed proposal system; it is supported by the U.S. Department of Energy, Office of Biological and Environmental Research.

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APS PDB Depositions from BioSync
SBC Sector 19 2013 2014 2015 TOTAL
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Beginning August 01, 2015 the Midwest Center for Structural Genomics (MCSG) will start accepting applications for access to the MCSG User Resource.


MCSG's structure determination platform is well established, and combines technologies, robotics and expertise for gene cloning, protein production, and crystallization, as well as biochemical and biophysical characterization.


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