5VPL

CRYSTAL STRUCTURE OF DER F 1 COMPLEXED WITH FAB 4C1

「3RVV」から置き換えられました

5VPL の概要

• エントリーDOI: 10.2210/pdb5vpl/pdb
• 関連するPDBエントリー: 5VPG 5VPH 5VPK
• 分子名称: Der f 1 variant, 4C1 - LIGHT CHAIN, 4C1 - HEAVY CHAIN, ... (7 entities in total)
• 機能のキーワード: complex between an allergen and fab fragment of 4c1 antibody, hydrolase-immune system complex, hydrolase/immune system
• 由来する生物種: Mus musculus (MOUSE); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 77295.45

構造登録者

Chruszcz, M.,Vailes, L.D.,Chapman, M.D.,Pomes, A.,Minor, W. (登録日: 2017-05-05, 公開日: 2017-05-24, 最終更新日: 2023-10-04)

主引用文献

Chruszcz, M.,Pomes, A.,Glesner, J.,Vailes, L.D.,Osinski, T.,Porebski, P.J.,Majorek, K.A.,Heymann, P.W.,Platts-Mills, T.A.,Minor, W.,Chapman, M.D.
Molecular Determinants For Antibody Binding On Group 1 House Dust Mite Allergens.
J.Biol.Chem., 287:7388-, 2012

PubMed Abstract: House dust mites produce potent allergens, Der p 1 and Der f 1, that cause allergic sensitization and asthma. Der p 1 and Der f 1 are cysteine proteases that elicit IgE responses in 80% of mite-allergic subjects and have proinflammatory properties. Their antigenic structure is unknown. Here, we present crystal structures of natural Der p 1 and Der f 1 in complex with a monoclonal antibody, 4C1, which binds to a unique cross-reactive epitope on both allergens associated with IgE recognition. The 4C1 epitope is formed by almost identical amino acid sequences and contact residues. Mutations of the contact residues abrogate mAb 4C1 binding and reduce IgE antibody binding. These surface-exposed residues are molecular targets that can be exploited for development of recombinant allergen vaccines.

PubMed: 22210776
DOI: 10.1074/JBC.M111.311159

実験手法

X-RAY DIFFRACTION (1.9 Å)