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Title | Cryo-EM structure of the PlexinC1/A39R complex reveals inter-domain interactions critical for ligand-induced activation. |
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Journal, issue, pages | Nat Commun, Vol. 11, Issue 1, Page 1953, Year 2020 |
Publish date | Apr 23, 2020 |
Authors | Yi-Chun Kuo / Hua Chen / Guijun Shang / Emiko Uchikawa / Hui Tian / Xiao-Chen Bai / Xuewu Zhang / |
PubMed Abstract | Plexins are receptors for semaphorins that transduce signals for regulating neuronal development and other processes. Plexins are single-pass transmembrane proteins with multiple domains in both the ...Plexins are receptors for semaphorins that transduce signals for regulating neuronal development and other processes. Plexins are single-pass transmembrane proteins with multiple domains in both the extracellular and intracellular regions. Semaphorin activates plexin by binding to its extracellular N-terminal Sema domain, inducing the active dimer of the plexin intracellular region. The mechanism underlying this activation process of plexin is incompletely understood. We present cryo-electron microscopic structure of full-length human PlexinC1 in complex with the viral semaphorin mimic A39R. The structure shows that A39R induces a specific dimer of PlexinC1 where the membrane-proximal domains from the two PlexinC1 protomers are placed close to each other, poised to promote the active dimer of the intracellular region. This configuration is imposed by a distinct conformation of the PlexinC1 extracellular region, stabilized by inter-domain interactions among the Sema and membrane-proximal domains. Our mutational analyses support the critical role of this conformation in PlexinC1 activation. |
External links | Nat Commun / PubMed:32327662 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.1 Å |
Structure data | EMDB-21442, PDB-6vxk: |
Chemicals | ChemComp-NAG: |
Source |
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Keywords | MEMBRANE PROTEIN / receptor / signaling / plexin |