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1osy
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(New page: 200px<br /><applet load="1osy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1osy, resolution 1.70Å" /> '''Crystal structure of...)
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Revision as of 21:02, 20 November 2007
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Crystal structure of FIP-Fve fungal immunomodulatory protein
Overview
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.
About this Structure
1OSY is a Single protein structure of sequence from Flammulina velutipes with BR and ACE as ligands. Full crystallographic information is available from OCA.
Reference
A 1.7A structure of Fve, a member of the new fungal immunomodulatory protein family., Paaventhan P, Joseph JS, Seow SV, Vaday S, Robinson H, Chua KY, Kolatkar PR, J Mol Biol. 2003 Sep 12;332(2):461-70. PMID:12948495
Page seeded by OCA on Tue Nov 20 23:09:55 2007
