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1osy
From Proteopedia
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| - | + | ==Crystal structure of FIP-Fve fungal immunomodulatory protein== | |
| - | + | <StructureSection load='1osy' size='340' side='right'caption='[[1osy]], [[Resolution|resolution]] 1.70Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | | | + | <table><tr><td colspan='2'>[[1osy]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OSY FirstGlance]. <br> |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene></td></tr> | |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1osy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1osy OCA], [https://pdbe.org/1osy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1osy RCSB], [https://www.ebi.ac.uk/pdbsum/1osy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1osy ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/FVE_FLAVE FVE_FLAVE] Lectin with specificity for complex cell-surface carbohydrates. Possesses 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. | |
| - | + | <div style="background-color:#fffaf0;"> | |
| - | + | == Publication Abstract from PubMed == | |
| - | == | + | |
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. | 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. | ||
| - | + | 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<ref>PMID:12948495</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 1osy" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Flammulina velutipes]] | [[Category: Flammulina velutipes]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Chua | + | [[Category: Chua KY]] |
| - | [[Category: Joseph | + | [[Category: Joseph JS]] |
| - | [[Category: Kolatkar | + | [[Category: Kolatkar PR]] |
| - | [[Category: Palasingam | + | [[Category: Palasingam P]] |
| - | [[Category: Robinson | + | [[Category: Robinson H]] |
| - | [[Category: Seow | + | [[Category: Seow SV]] |
| - | [[Category: Shai | + | [[Category: Shai V]] |
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Current revision
Crystal structure of FIP-Fve fungal immunomodulatory protein
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