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Structure, dynamics and stability of allergen cod parvalbumin Gad m 1 by solution and high-pressure NMR.Structure, dynamics and stability of allergen cod parvalbumin Gad m 1 by solution and high-pressure NMR.
Structural highlights
FunctionPRVB_GADMO In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions (By similarity). Publication Abstract from PubMedBeta-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. Proteins 2014; 82:3032-3042. (c) 2014 Wiley Periodicals, Inc. Solution and high-pressure NMR studies of the structure, dynamics, and stability of the cross-reactive allergenic cod parvalbumin Gad m 1.,Moraes AH, Ackerbauer D, Kostadinova M, Bublin M, de Oliveira GA, Ferreira F, Almeida FC, Breiteneder H, Valente AP Proteins. 2014 Nov;82(11):3032-42. doi: 10.1002/prot.24664. Epub 2014 Aug 30. PMID:25116395[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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