5em1: Difference between revisions
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==Crystal structure of ragweed allergen Amb a 8== | |||
<StructureSection load='5em1' size='340' side='right' caption='[[5em1]], [[Resolution|resolution]] 1.45Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5em1]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EM1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EM1 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BEZ:BENZOIC+ACID'>BEZ</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5em0|5em0]]</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5em1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5em1 OCA], [http://pdbe.org/5em1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5em1 RCSB], [http://www.ebi.ac.uk/pdbsum/5em1 PDBsum]</span></td></tr> | |||
</table> | |||
== 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] | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:27231348</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5em1" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Chruszcz, M]] | [[Category: Chruszcz, M]] | ||
[[Category: Offermann, L | [[Category: He, J Z]] | ||
[[Category: Offermann, L R]] | |||
[[Category: Perdue, M L]] | |||
[[Category: Allergen]] | |||
Revision as of 18:22, 20 June 2016
Crystal structure of ragweed allergen Amb a 8Crystal structure of ragweed allergen Amb a 8
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 PubMedRagweed 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. References
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