1osy

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[[Image:1osy.jpg|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1osy", creates the "Structure Box" on the page.
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{{STRUCTURE_1osy| PDB=1osy | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1osy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1osy OCA], [http://www.ebi.ac.uk/pdbsum/1osy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1osy RCSB]</span>
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'''Crystal structure of FIP-Fve fungal immunomodulatory protein'''
'''Crystal structure of FIP-Fve fungal immunomodulatory protein'''
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[[Category: Seow, S V.]]
[[Category: Seow, S V.]]
[[Category: Shai, V.]]
[[Category: Shai, V.]]
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[[Category: fibronectin fold]]
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[[Category: Fibronectin fold]]
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[[Category: fungal protein]]
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[[Category: Fungal protein]]
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[[Category: hemagglutination]]
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[[Category: Hemagglutination]]
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[[Category: immunomodulatory]]
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[[Category: Immunomodulatory]]
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[[Category: lectin]]
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[[Category: Lectin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:14:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:49:54 2008''
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Revision as of 01:14, 3 May 2008

Template:STRUCTURE 1osy

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. 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 Sat May 3 04:14:39 2008

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