We found a match
Your institution may have rights to this item. Sign in to continue.
- Title
Solution structure of Phl p 3, a major allergen from timothy grass pollen.
- Authors
Schweimer, Kristian; Petersen, Arnd; Suck, Roland; Becker, Wolf-Meinhard; Rösch, Paul; Matecko, Irena
- Abstract
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 β-sheets of five and four anti-parallel β-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.
- Subjects
ALLERGENS; POLLEN; EPITOPES; GRASSES; PLANT extracts; IMMUNOGLOBULIN E
- Publication
Biological Chemistry, 2008, Vol 389, Issue 7, p919
- ISSN
1431-6730
- Publication type
Article
- DOI
10.1515/BC.2008.102