1osy: Difference between revisions
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'''Crystal structure of FIP-Fve fungal immunomodulatory protein''' | {{Structure | ||
|PDB= 1osy |SIZE=350|CAPTION= <scene name='initialview01'>1osy</scene>, resolution 1.70Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene> and <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal structure of FIP-Fve fungal immunomodulatory protein''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1OSY is a [ | 1OSY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Flammulina_velutipes Flammulina velutipes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OSY OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12948495 12948495] | ||
[[Category: Flammulina velutipes]] | [[Category: Flammulina velutipes]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: lectin]] | [[Category: lectin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:15:19 2008'' | ||
Revision as of 11:15, 20 March 2008
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| 1osy, resolution 1.70Å | |||||||||||||
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| Ligands: | BR and ACE | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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