2MBX

Structure, dynamics and stability of allergen cod parvalbumin Gad m 1 by solution and high-pressure NMR.

2MBX の概要

• エントリーDOI: 10.2210/pdb2mbx/pdb
• NMR情報: BMRB: 18113
• 分子名称: Parvalbumin beta, CALCIUM ION (2 entities in total)
• 機能のキーワード: allergen, parvalbumin, ef-hand, contractile protein
• 由来する生物種: Gadus morhua (Atlantic cod)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11645.20

構造登録者

Moraes, A.H.,Ackerbauer, D.,Bublin, M.,Ferreira, F.,Almeida, F.C.L.,Breiteneder, H.,Valente, A. (登録日: 2013-08-07, 公開日: 2014-08-20, 最終更新日: 2024-05-15)

主引用文献

Moraes, A.H.,Ackerbauer, D.,Kostadinova, M.,Bublin, M.,de Oliveira, G.A.,Ferreira, F.,Almeida, F.C.,Breiteneder, H.,Valente, A.P.
Solution and high-pressure NMR studies of the structure, dynamics, and stability of the cross-reactive allergenic cod parvalbumin Gad m 1.
Proteins, 82:3032-3042, 2014

PubMed Abstract: Beta-parvalbumins from different fish species have been identified as the main elicitors of IgE-mediated reactions in fish-allergic individuals. Here, we report for the first time the NMR determination of the structure and dynamics of the major Atlantic cod (Gadus morhua) allergen Gad m 1 and compare them with other known parvalbumins. Although the Gad m 1 structure and accessibility of putative IgE epitopes are similar to parvalbumins in mackerel and carp, the charge distribution at the putative epitopes is different. The determination of the Gad m 1 structure contributes to a better understanding of cross-reactivity among fish parvalbumins. In addition, the high-pressure NMR and temperature variation experiments revealed the important contribution of the AB motif and other regions to the protein folding. This structural information could assist the future identification of hot spots for targeted mutations to develop hypoallergenic Ca(2+) -free forms for potential use in immunotherapy.

PubMed: 25116395
DOI: 10.1002/prot.24664

実験手法

SOLUTION NMR