5ev0

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'''Unreleased structure'''
 
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The entry 5ev0 is ON HOLD until Paper Publication
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==Crystal structure of ragweed profilin Amb a 8 in complex with poly-Pro14==
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<StructureSection load='5ev0' size='340' side='right' caption='[[5ev0]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5ev0]] is a 4 chain structure. 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EV0 FirstGlance]. <br>
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</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>
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<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=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]</span></td></tr>
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</table>
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== Function ==
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[[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]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors:
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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>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5ev0" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Chruszcz, M]]
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[[Category: He, J Z]]
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[[Category: Offermann, L R]]
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[[Category: Perdue, M L]]
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[[Category: Allergen]]

Revision as of 15:22, 20 June 2016

Crystal structure of ragweed profilin Amb a 8 in complex with poly-Pro14

5ev0, resolution 2.10Å

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