کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2525926 1119653 2007 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
The intrinsic flexibility of IgE and its role in binding FcɛRI
موضوعات مرتبط
علوم پزشکی و سلامت پزشکی و دندانپزشکی تومور شناسی
پیش نمایش صفحه اول مقاله
The intrinsic flexibility of IgE and its role in binding FcɛRI
چکیده انگلیسی

The interaction between IgE and its high affinity cellular receptor (FcɛRI) is an essential step in the development of allergic responses. Studies have identified the third constant domain of IgE (Cɛ3) as the receptor binding region. The Cɛ3 domain has unusual structural features; it was found to be a ‘molten globule’ structure in an isolated form, only assuming a well structured form upon binding to FcɛRI. The conformational flexibility intrinsic to the receptor binding portion of the molecule may be useful to IgE in allowing the large allosteric changes postulated to be required for FcɛRI engagement. If allosteric inhibitors can be developed then the dynamic properties of the Cɛ3 domain may provide opportunities for therapeutic intervention in allergic disorders.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biomedicine & Pharmacotherapy - Volume 61, Issue 1, January 2007, Pages 61–67
نویسندگان
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