5eve | pdb_00005eve
Crystal structure of Amb a 8 in complex with poly-Pro10
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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