1osy
From Proteopedia
(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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| - | [[Image:1osy.jpg|left|200px]]<br /><applet load="1osy" size=" | + | [[Image:1osy.jpg|left|200px]]<br /><applet load="1osy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1osy, resolution 1.70Å" /> | caption="1osy, resolution 1.70Å" /> | ||
'''Crystal structure of FIP-Fve fungal immunomodulatory protein'''<br /> | '''Crystal structure of FIP-Fve fungal immunomodulatory protein'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Fve, a major fruiting body protein from Flammulina velutipes, a mushroom | + | 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== | ==About this Structure== | ||
| - | 1OSY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Flammulina_velutipes Flammulina velutipes] with BR and ACE as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1OSY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Flammulina_velutipes Flammulina velutipes] with <scene name='pdbligand=BR:'>BR</scene> and <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OSY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Flammulina velutipes]] | [[Category: Flammulina velutipes]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Chua, K | + | [[Category: Chua, K Y.]] |
| - | [[Category: Joseph, J | + | [[Category: Joseph, J S.]] |
| - | [[Category: Kolatkar, P | + | [[Category: Kolatkar, P R.]] |
[[Category: Palasingam, P.]] | [[Category: Palasingam, P.]] | ||
[[Category: Robinson, H.]] | [[Category: Robinson, H.]] | ||
| - | [[Category: Seow, S | + | [[Category: Seow, S V.]] |
[[Category: Shai, V.]] | [[Category: Shai, V.]] | ||
[[Category: ACE]] | [[Category: ACE]] | ||
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[[Category: lectin]] | [[Category: lectin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:21:14 2008'' |
Revision as of 12:21, 21 February 2008
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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 and 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
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