Solution structure of Phl p 3, a major allergen from timothy grass pollen.
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.
Schweimer
Kristian
K
Lehrstuhl Biopolymere und Forschungszentrum für Bio-Makromoleküle, Universität Bayreuth, Universitätsstr. 30, Bayreuth, Germany.
Petersen
Arnd
A
Suck
Roland
R
Becker
Wolf-Meinhard
WM
Rösch
Paul
P
Matecko
Irena
I
D000485:Allergens / Q000737:chemistry* / Q000276:immunology / Q000302:isolation & purification; D000595:Amino Acid Sequence; D052179:Antigens, Plant / Q000737:chemistry* / Q000276:immunology / Q000302:isolation & purification*; D000939:Epitopes / Q000737:chemistry / Q000276:immunology; D007073:Immunoglobulin E / Q000276:immunology; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D031784:Phleum / Q000737:chemistry* / Q000276:immunology; D011058:Pollen / Q000737:chemistry* / Q000276:immunology; D011487:Protein Conformation; D055672:Static Electricity
D000485:Allergens; D052179:Antigens, Plant; D000939:Epitopes; C514376:Phl p 3 allergen, Phleum pratense; D007073:Immunoglobulin E