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1osy
From Proteopedia
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|PDB= 1osy |SIZE=350|CAPTION= <scene name='initialview01'>1osy</scene>, resolution 1.70Å | |PDB= 1osy |SIZE=350|CAPTION= <scene name='initialview01'>1osy</scene>, resolution 1.70Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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[[Category: Seow, S V.]] | [[Category: Seow, S V.]] | ||
[[Category: Shai, V.]] | [[Category: Shai, V.]] | ||
| - | [[Category: ACE]] | ||
| - | [[Category: BR]] | ||
[[Category: fibronectin fold]] | [[Category: fibronectin fold]] | ||
[[Category: fungal protein]] | [[Category: fungal protein]] | ||
| Line 37: | Line 38: | ||
[[Category: lectin]] | [[Category: lectin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:49:54 2008'' |
Revision as of 19:49, 30 March 2008
| |||||||
| , resolution 1.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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