3NVN

Molecular mechanism of guidance cue recognition

Summary for 3NVN

• Entry DOI: 10.2210/pdb3nvn/pdb
• Related: 3NVQ 3NVX
• Descriptor: EVM139, Plexin-C1, 2-acetamido-2-deoxy-alpha-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: beta-propeller, signaling, viral protein-signaling protein complex, viral protein/signaling protein
• Biological source: Ectromelia virus; More
• Cellular location: Membrane; Single-pass type I membrane protein (Potential): O60486
• Total number of polymer chains: 2
• Total formula weight: 97647.69

Authors

Liu, H.,Juo, Z.,Shim, A.,Focia, P.,Chen, X.,Garcia, C.,He, X. (deposition date: 2010-07-08, release date: 2010-09-15, Last modification date: 2024-10-30)

Primary citation

Liu, H.,Juo, Z.S.,Shim, A.H.,Focia, P.J.,Chen, X.,Garcia, K.C.,He, X.
Structural Basis of Semaphorin-Plexin Recognition and Viral Mimicry from Sema7A and A39R Complexes with PlexinC1.
Cell(Cambridge,Mass.), 142:749-761, 2010

PubMed Abstract: Repulsive signaling by Semaphorins and Plexins is crucial for the development and homeostasis of the nervous, immune, and cardiovascular systems. Sema7A acts as both an immune and a neural Semaphorin through PlexinC1, and A39R is a Sema7A mimic secreted by smallpox virus. We report the structures of Sema7A and A39R complexed with the Semaphorin-binding module of PlexinC1. Both structures show two PlexinC1 molecules symmetrically bridged by Semaphorin dimers, in which the Semaphorin and PlexinC1 beta propellers interact in an edge-on, orthogonal orientation. Both binding interfaces are dominated by the insertion of the Semaphorin's 4c-4d loop into a deep groove in blade 3 of the PlexinC1 propeller. A39R appears to achieve Sema7A mimicry by preserving key Plexin-binding determinants seen in the mammalian Sema7A complex that have evolved to achieve higher affinity binding to the host-derived PlexinC1. The complex structures support a conserved Semaphorin-Plexin recognition mode and suggest that Plexins are activated by dimerization.

PubMed: 20727575
DOI: 10.1016/j.cell.2010.07.040

Experimental method

X-RAY DIFFRACTION (2.26 Å)