at Google ScholarTitle data
Schweimer, Kristian ; Petersen, Arnd ; Suck, Roland ; Becker, Wolf-Meinhard ; Rösch, Paul ; Matecko, Irena:
Solution structure of Phl p 3, a major allergen from timothy grass pollen.
In: Biological Chemistry.
Vol. 389
(2008)
Issue 7
.
- pp. 919-923.
ISSN 1437-4315
DOI: https://doi.org/10.1515/BC.2008.102
Abstract in another language
The major 97-aa timothy grass (Phleum pratense) allergen Phl p 3 was recently isolated from an extract of timothy grass pollen. Sequence comparison classifies this protein as a group 3 allergen. The solution structure of Phl p 3 as determined by nuclear magnetic resonance spectroscopy reveals that the protein consists of a core of hydrophobic amino-acid side chains from two beta-sheets of five and four anti-parallel beta-strands, respectively. This conformation is very similar to the crystal structure published for Phl p 2 and strongly resembles the known conformation of the carboxy-terminal domain of Phl p 1, the major difference being the loop orientations. Phl p 2 and Phl p 3 show virtually identical immunoreactivity, and comparison of the charged surface amino acids of the two proteins gives initial clues as to the IgE recognition epitopes of these proteins.