3H4Z

Crystal Structure of an MBP-Der p 7 fusion protein

3H4Z の概要

• エントリーDOI: 10.2210/pdb3h4z/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: Maltose-binding periplasmic protein fused with Allergen DERP7, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: mbp fusion, derp7, aha1/bpi domain-like, super roll, sugar transport, transport, allergen
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Secreted: P49273
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 188095.45

構造登録者

Pedersen, L.C.,Mueller, G.A.,London, R.E. (登録日: 2009-04-21, 公開日: 2010-03-31, 最終更新日: 2023-09-06)

主引用文献

Mueller, G.A.,Edwards, L.L.,Aloor, J.J.,Fessler, M.B.,Glesner, J.,Pomes, A.,Chapman, M.D.,London, R.E.,Pedersen, L.C.
The structure of the dust mite allergen Der p 7 reveals similarities to innate immune proteins.
J.Allergy Clin.Immunol., 125:909-917.e4, 2010

PubMed Abstract: Sensitization to house dust mite allergens is strongly correlated with asthma. Der p 7 elicits strong IgE antibody and T-cell responses in patients with mite allergy. However, the structure and biological function of this important allergen are unknown. Allergen function might contribute to allergenicity, as shown for the protease activity of group 1 mite allergens and the interaction with the innate immune system by group 2 mite allergens.

PubMed: 20226507
DOI: 10.1016/j.jaci.2009.12.016

実験手法

X-RAY DIFFRACTION (2.35 Å)