X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1110031
- author
- 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
- publishing date
- 1996
- 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
- 2016-04-01 16:17:47
- date last changed
- 2022-03-14 23:24:33
@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}}, doi = {{10.1038/nsb1296-1040}}, volume = {{3}}, year = {{1996}}, }