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| <StructureSection load='5ev0' size='340' side='right'caption='[[5ev0]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='5ev0' size='340' side='right'caption='[[5ev0]], [[Resolution|resolution]] 2.10Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[5ev0]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ambar Ambar]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EV0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5EV0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ev0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Ambrosia_artemisiifolia Ambrosia artemisiifolia] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EV0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EV0 FirstGlance]. <br> |
- | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5ev0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ev0 OCA], [http://pdbe.org/5ev0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ev0 RCSB], [http://www.ebi.ac.uk/pdbsum/5ev0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ev0 ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</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=5ev0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ev0 OCA], [https://pdbe.org/5ev0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ev0 RCSB], [https://www.ebi.ac.uk/pdbsum/5ev0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ev0 ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/Q2KN24_AMBAR Q2KN24_AMBAR]] Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations.[RuleBase:RU003908] | + | [https://www.uniprot.org/uniprot/Q2KN24_AMBAR Q2KN24_AMBAR] Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations.[RuleBase:RU003908] |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Ambar]] | + | [[Category: Ambrosia artemisiifolia]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Chruszcz, M]] | + | [[Category: Synthetic construct]] |
- | [[Category: He, J Z]] | + | [[Category: Chruszcz M]] |
- | [[Category: Offermann, L R]] | + | [[Category: He JZ]] |
- | [[Category: Perdue, M L]] | + | [[Category: Offermann LR]] |
- | [[Category: Allergen]] | + | [[Category: Perdue ML]] |
| Structural highlights
Function
Q2KN24_AMBAR Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations.[RuleBase:RU003908]
Publication Abstract from PubMed
Ragweed allergens affect several million people in the USA and Canada. To date, only two ragweed allergens, Amb t 5 and Amb a 11, have their structures determined and deposited to the Protein Data Bank. Here, we present structures of methylated ragweed allergen Amb a 8, Amb a 8 in the presence of poly-L-proline and Art v 4 (mugwort allergen). Amb a 8 and Art v 4 are panallergens belonging to the profilin family of proteins. They share significant sequence and structural similarities which results in cross-recognition by IgE antibodies. Molecular and immunological properties of Amb a 8 and Art v 4 are compared to those of Bet v 2 (birch pollen allergen), as well as to other allergenic profilins. We purified recombinant allergens that are recognized by patient IgE and are highly cross-reactive. It was determined that the analyzed allergens are relatively unstable. Structures of Amb a 8 in complex with poly-L-proline10 or poly-L-proline14 are the first structures of the plant profilin in complex with proline-rich peptides. Amb a 8 binds the poly-L-proline in a mode similar to that observed in human, mouse and P. falciparum profilin-peptide complexes. However, only some of residues that form the peptide binding site are conserved.
Structural, functional and immunological characterization of profilin panallergens amb a 8, Art v 4, and Bet v 2.,Offermann LR, Schlachter CR, Perdue ML, Majorek KA, He JZ, Booth WT, Garrett J, Kowal K, Chruszcz M J Biol Chem. 2016 May 26. pii: jbc.M116.733659. PMID:27231348[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Offermann LR, Schlachter CR, Perdue ML, Majorek KA, He JZ, Booth WT, Garrett J, Kowal K, Chruszcz M. Structural, functional and immunological characterization of profilin panallergens amb a 8, Art v 4, and Bet v 2. J Biol Chem. 2016 May 26. pii: jbc.M116.733659. PMID:27231348 doi:http://dx.doi.org/10.1074/jbc.M116.733659
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