3nvx

Molecular mechanism of guidance cue recognition

spinqualitylabelsall models 3nvx, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3nvx is a 2 chain structure with sequence from Vaccinia virus Copenhagen. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SEMA_VACCC Acts as a semaphorin-like protein and binds to host plexin C1 receptor. May alter the movement of host plexin C1-expressing cells including dendritic cells, monocytes, or granulocytes in the proximity of infected cells. May also regulate host cell cytoskeleton of neighboring cells to improve viral infection (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structural basis of semaphorin-plexin recognition and viral mimicry from Sema7A and A39R complexes with PlexinC1.,Liu H, Juo ZS, Shim AH, Focia PJ, Chen X, Garcia KC, He X Cell. 2010 Sep 3;142(5):749-61. Epub 2010 Aug 19. PMID:20727575 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Semaphorin 3D structures

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