5EV0

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

Summary for 5EV0

• Entry DOI: 10.2210/pdb5ev0/pdb
• Descriptor: Profilin, PRO-PRO-PRO-PRO-PRO-PRO-PRO-PRO-PRO (3 entities in total)
• Functional Keywords: allergen
• Biological source: Ambrosia artemisiifolia (Short ragweed); More
• Total number of polymer chains: 4
• Total formula weight: 30476.72

Authors

Offermann, L.R.,He, J.Z.,Perdue, M.L.,Chruszcz, M. (deposition date: 2015-11-19, release date: 2016-06-08, Last modification date: 2024-10-16)

Primary citation

Offermann, L.R.,Schlachter, C.R.,Perdue, M.L.,Majorek, K.A.,He, J.Z.,Booth, W.T.,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., 291:15447-15459, 2016

PubMed Abstract: Ragweed allergens affect several million people in the United States 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 with those of Bet v 2 (birch pollen allergen) as well as with 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-proline)10 or poly(l-proline)14 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 the residues that form the peptide binding site are conserved.

PubMed: 27231348
DOI: 10.1074/jbc.M116.733659

Experimental method

X-RAY DIFFRACTION (2.1 Å)