Restricted Motion of the Conserved Immunoglobulin G1 N-Glycan Is Essential for Efficient FcγRIIIa Binding
نویسندگان
چکیده
منابع مشابه
The role of the Immunoglobulin G1 Fc N-glycan in FcÎ3RIIIa affinity
IgG1 Fc is a remarkable molecule, capable of initiating pro-inflammatory or antiinflammatory responses by binding to Fc receptors. IgG1 Fc has a conserved glycosylation site at N297. The presence of the carbohydrate at N297 is vital for proper Fc function. Intramolecular glycan-polypeptide interactions are thought to impose conformational restrictions on Fc that maintain binding-favorable inter...
متن کاملIntramolecular N-Glycan/Polypeptide Interactions Observed at Multiple N-Glycan Remodeling Steps through [13C,15N]-N-Acetylglucosamine Labeling of Immunoglobulin G1
Asparagine-linked (N) glycosylation is a common eukaryotic protein modification that affects protein folding, function, and stability through intramolecular interactions between N-glycan and polypeptide residues. Attempts to characterize the structure-activity relationship of each N-glycan are hindered by inherent properties of the glycoprotein, including glycan conformational and compositional...
متن کاملnano-rods zno as an efficient catalyst for the synthesis of chromene phosphonates, direct amidation and formylation of amines
چکیده ندارد.
Conserved arginine-516 of Penicillium amagasakiense glucose oxidase is essential for the efficient binding of beta-D-glucose.
The effects of mutation of key conserved active-site residues (Tyr-73, Phe-418, Trp-430, Arg-516, Asn-518, His-520 and His-563) of glucose oxidase from Penicillium amagasakiense on substrate binding were investigated. Kinetic studies on the oxidation of beta-D-glucose combined with molecular modelling showed the side chain of Arg-516, which forms two hydrogen bonds with the 3-OH group of beta-D...
متن کاملComprehensive N-Glycan Profiling of Avian Immunoglobulin Y
Recent exploitation of the avian immune system has highlighted its suitability for the generation of high-quality, high-affinity antibodies to a wide range of antigens for a number of therapeutic and biotechnological applications. The glycosylation profile of potential immunoglobulin therapeutics is species specific and is heavily influenced by the cell-line/culture conditions used for producti...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Structure
سال: 2014
ISSN: 0969-2126
DOI: 10.1016/j.str.2014.08.002