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|Title:||A 1.7 Å structure of Fve, a member of the new fungal immunomodulatory protein family|
|Keywords:||3-D domain swapping|
Fungal immunomodulatory protein
|Citation:||Paaventhan, P., Joseph, J.S., Kolatkar, P.R., Seow, S.V., Chua, K.Y., Vaday, S., Robinson, H. (2003). A 1.7 Å structure of Fve, a member of the new fungal immunomodulatory protein family. Journal of Molecular Biology 332 (2) : 461-470. ScholarBank@NUS Repository. https://doi.org/10.1016/S0022-2836(03)00923-9|
|Abstract:||Fve, a major fruiting body protein from Flammulina velutipes, a mushroom possessing immunomodulatory activity, stimulates lymphocyte mitogenesis, suppresses systemic anaphylaxis reactions and edema, enhances transcription of IL-2, IFN-γ and TNF-α, and hemagglutinates red blood cells. It appears to be a lectin with specificity for complex cell-surface carbohydrates. Fve is a non-covalently linked homodimer containing no Cys, His or Met residues. It shares sequence similarity only to the other fungal immunomodulatory proteins (FIPs) LZ-8, Gts, Vvo and Vvl, all of unknown structure. The 1. 7Å structure of Fve solved by single anomalous diffraction of NaBr-soaked crystals is novel: each monomer consists of an N-terminal α-helix followed by a fibronectin III (FNIII) fold. The FNIII fold is the first instance of "pseudo-h-type" topology, a transition between the seven β-stranded s-type and the eight β-stranded h-type topologies. The structure suggests that dimerization, critical for the activity of FIPs, occurs by 3-D domain swapping of the N-terminal helices and is stabilized predominantly by hydrophobic interactions. The structure of Fve is the first in this lectin family to be reported, and the first of an FNIII domain-containing protein of fungal origin. © 2003 Elsevier Ltd. All rights reserved.|
|Source Title:||Journal of Molecular Biology|
|Appears in Collections:||Staff Publications|
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