6fkk

Drosophila Semaphorin 1b, extracellular domains 1-2

spinqualitylabelsall models 6fkk, resolution 2.78Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6fkk is a 1 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.78Å Ligands: BMA, MAN, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q7KK54_DROME Publication Abstract from PubMed Semaphorin ligands and their plexin receptors are one of the major cell guidance factors that trigger localised changes in the cytoskeleton. Binding of semaphorin homodimer to plexin brings two plexins in close proximity which is a prerequisite for plexin signalling. This model appears to be too simplistic to explain the complexity and functional versatility of these molecules. Here, we determine crystal structures for all members of Drosophila class 1 and 2 semaphorins. Unlike previously reported semaphorin structures, Sema1a, Sema2a and Sema2b show stabilisation of sema domain dimer formation via a disulfide bond. Unexpectedly, our structural and biophysical data show Sema1b is a monomer suggesting that semaphorin function may not be restricted to dimers. We demonstrate that semaphorins can form heterodimers with members of the same semaphorin class. This heterodimerization provides a potential mechanism for cross-talk between different plexins and co-receptors to allow fine-tuning of cell signalling. Diversity of oligomerization in Drosophila semaphorins suggests a mechanism of functional fine-tuning.,Rozbesky D, Robinson RA, Jain V, Renner M, Malinauskas T, Harlos K, Siebold C, Jones EY Nat Commun. 2019 Aug 15;10(1):3691. doi: 10.1038/s41467-019-11683-y. PMID:31417095 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Semaphorin 3D structures

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