1osy: Difference between revisions

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{{STRUCTURE_1osy|  PDB=1osy  |  SCENE=  }}  
{{STRUCTURE_1osy|  PDB=1osy  |  SCENE=  }}  


'''Crystal structure of FIP-Fve fungal immunomodulatory protein'''
===Crystal structure of FIP-Fve fungal immunomodulatory protein===




==Overview==
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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-gamma and TNF-alpha, 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 1.7A structure of Fve solved by single anomalous diffraction of NaBr-soaked crystals is novel: each monomer consists of an N-terminal alpha-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 beta-stranded s-type and the eight beta-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.
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{{ABSTRACT_PUBMED_12948495}}


==About this Structure==
==About this Structure==
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[[Category: Immunomodulatory]]
[[Category: Immunomodulatory]]
[[Category: Lectin]]
[[Category: Lectin]]
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