4j4p

Publication Abstract from PubMed

Crystallographic and solution studies have shown that IgE molecules are acutely bent in their Fc region. Crystal structures reveal the Cvarepsilon2 domain pair folded back onto the Cvarepsilon3-Cvarepsilon4 domains, but is the molecule exclusively bent or can the Cvarepsilon2 domains adopt extended conformations and even 'flip' from one side of the molecule to the other? We report the crystal structure of IgE-Fc captured in a fully extended, symmetrical conformation and show by molecular dynamics, calorimetry, stopped-flow kinetic, surface plasmon resonance (SPR) and Forster resonance energy transfer (FRET) analyses that the antibody can indeed adopt such extended conformations in solution. This diversity of conformational states available to IgE-Fc offers a new perspective on IgE function in allergen recognition, as part of the B-cell receptor and as a therapeutic target in allergic disease.

Human immunoglobulin E flexes between acutely bent and extended conformations.,Drinkwater N, Cossins BP, Keeble AH, Wright M, Cain K, Hailu H, Oxbrow A, Delgado J, Shuttleworth LK, Kao MW, McDonnell JM, Beavil AJ, Henry AJ, Sutton BJ Nat Struct Mol Biol. 2014 Apr;21(4):397-404. doi: 10.1038/nsmb.2795. Epub 2014, Mar 16. PMID:24632569^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.