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

Structure(2016)

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Abstract
(Structure 23, 1678–1691, September 1, 2015) Nan-Sheng Li (of the Department of Biochemistry and Molecular Biology at the University of Chicago, Chicago, IL) had previously synthesized the reagent “Biotin-tris-nitrilotriacetic acid” that was used in some of the experiments in this manuscript. The authors regret that Nan-Sheng Li’s name was omitted inadvertently from the author list. The corrected author list is printed above, and the corrected article has been posted online. Structural Basis of Latrophilin-FLRT-UNC5 Interaction in Cell AdhesionLu et al.StructureJuly 30, 2015In BriefFLRTs, LPHNs, and UNC5s are families of interacting neuronal cell-surface receptors that mediate brain development. The LPHN3/FLRT3 structure, reported by Lu et al., reveals that LPHN3 binds to FLRT3 at a site distinct from UNC5. FLRT3 simultaneously binds to LPHN3 and UNC5, and forms a trimeric complex. Full-Text PDF Open Archive
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Key words
cell adhesion,latrophilin-flrt-unc
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