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3NVQ

Molecular mechanism of guidance cue recognition

Summary for 3NVQ
Entry DOI10.2210/pdb3nvq/pdb
Related3NVX 3nvn
DescriptorSemaphorin-7A, Plexin-C1, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
Functional Keywordsbeta-propeller, signaling, signaling protein-protein binding complex, signaling protein/protein binding
Biological sourceHomo sapiens (human)
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Total number of polymer chains4
Total formula weight242651.05
Authors
Juo, Z.,Liu, H.,Shim, A.,Focia, P.,Chen, X.,Garcia, C.,He, X. (deposition date: 2010-07-08, release date: 2010-09-15, Last modification date: 2020-07-29)
Primary citationLiu, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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