X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy
Författare
Summary, in English
The three-dimensional structure of the major birch pollen allergen, the 17,500 M(r) acidic protein Bet v 1 (from the birch, Betula verrucosa), is presented as determined both in the crystalline state by X-ray diffraction and in solution by nuclear magnetic resonance (NMR) spectroscopy. This is the first experimentally determined structure of a clinically important inhalant major allergen, estimated to cause allergy in 5-10 million individuals worldwide. The structure shows three regions on the molecular surface predicted to harbour cross-reactive B-cell epitopes which provide a structural basis for the allergic symptoms that birch pollen allergic patients show when they encounter pollens from related trees such as hazel, alder and hornbeam. The structure also shows an unusual feature, a 30 A-long forked cavity that penetrates the entire protein.
Publiceringsår
1996
Språk
Engelska
Sidor
1040-1045
Publikation/Tidskrift/Serie
Nature Structural Biology
Volym
3
Issue
12
Dokumenttyp
Artikel i tidskrift
Förlag
Nature Publishing Group
Ämne
- Endocrinology and Diabetes
Status
Published
ISBN/ISSN/Övrigt
- ISSN: 1072-8368