1BV1

BIRCH POLLEN ALLERGEN BET V 1

1BV1 の概要

• エントリーDOI: 10.2210/pdb1bv1/pdb
• 分子名称: BET V 1 (2 entities in total)
• 機能のキーワード: allergen, pathogenesis-related protein
• 由来する生物種: Betula pendula (European white birch)
• 細胞内の位置: Cytoplasm: P15494
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17427.58

構造登録者

Gajhede, M.,Osmark, P.,Poulsen, F.M.,Ipsen, H.,Larson, J.N.,Joostvan, R.J.,Schou, C.,Lowenstein, H.,Spangfort, M.D. (登録日: 1997-07-08, 公開日: 1997-09-17, 最終更新日: 2024-02-07)

主引用文献

Gajhede, M.,Osmark, P.,Poulsen, F.M.,Ipsen, H.,Larsen, J.N.,Joost van Neerven, R.J.,Schou, C.,Lowenstein, H.,Spangfort, M.D.
X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy.
Nat.Struct.Biol., 3:1040-1045, 1996

PubMed 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.

PubMed: 8946858
DOI: 10.1038/nsb1296-1040

実験手法

X-RAY DIFFRACTION (2 Å)