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6FKM

Drosophila Plexin A in complex with Semaphorin 1b

Summary for 6FKM
Entry DOI10.2210/pdb6fkm/pdb
DescriptorPlexin A, isoform A, MIP07328p, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
Functional Keywordssemaphorin, plexin, sema domain, cell-cell signaling, signaling protein
Biological sourceDrosophila melanogaster (Fruit fly)
More
Total number of polymer chains2
Total formula weight145618.29
Authors
Rozbesky, D.,Harlos, K.,Jones, E.Y. (deposition date: 2018-01-24, release date: 2019-02-06, Last modification date: 2024-01-17)
Primary citationRozbesky, D.,Verhagen, M.G.,Karia, D.,Nagy, G.N.,Alvarez, L.,Robinson, R.A.,Harlos, K.,Padilla-Parra, S.,Pasterkamp, R.J.,Jones, E.Y.
Structural basis of semaphorin-plexin cis interaction.
Embo J., :e102926-e102926, 2020
Cited by
PubMed Abstract: Semaphorin ligands interact with plexin receptors to contribute to functions in the development of myriad tissues including neurite guidance and synaptic organisation within the nervous system. Cell-attached semaphorins interact in trans with plexins on opposing cells, but also in cis on the same cell. The interplay between trans and cis interactions is crucial for the regulated development of complex neural circuitry, but the underlying molecular mechanisms are uncharacterised. We have discovered a distinct mode of interaction through which the Drosophila semaphorin Sema1b and mouse Sema6A mediate binding in cis to their cognate plexin receptors. Our high-resolution structural, biophysical and in vitro analyses demonstrate that monomeric semaphorins can mediate a distinctive plexin binding mode. These findings suggest the interplay between monomeric vs dimeric states has a hereto unappreciated role in semaphorin biology, providing a mechanism by which Sema6s may balance cis and trans functionalities.
PubMed: 32500924
DOI: 10.15252/embj.2019102926
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.96 Å)
Structure validation

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