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X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy

Gajhede, M; Osmark, Peter LU ; Poulsen, F M; Ipsen, H; Larsen, J N; Joost van Neerven, R J; Schou, C; Lowenstein, H and Spangfort, M D (1996) In Nature Structural Biology 3(12). p.1040-1045
Abstract
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... (More)
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. (Less)
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author
publishing date
type
Contribution to journal
publication status
published
subject
in
Nature Structural Biology
volume
3
issue
12
pages
1040 - 1045
publisher
Nature Publishing Group
external identifiers
  • pmid:8946858
  • scopus:0030471602
ISSN
1072-8368
DOI
10.1038/nsb1296-1040
language
English
LU publication?
no
id
dbe9ac27-146c-4d56-a150-ec97c587b527 (old id 1110031)
date added to LUP
2008-07-23 10:06:02
date last changed
2017-08-06 04:32:29
@article{dbe9ac27-146c-4d56-a150-ec97c587b527,
  abstract     = {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.},
  author       = {Gajhede, M and Osmark, Peter and Poulsen, F M and Ipsen, H and Larsen, J N and Joost van Neerven, R J and Schou, C and Lowenstein, H and Spangfort, M D},
  issn         = {1072-8368},
  language     = {eng},
  number       = {12},
  pages        = {1040--1045},
  publisher    = {Nature Publishing Group},
  series       = {Nature Structural Biology},
  title        = {X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy},
  url          = {http://dx.doi.org/10.1038/nsb1296-1040},
  volume       = {3},
  year         = {1996},
}