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From Proteopedia
IgG1 Fc-FcgammaRI ecd complex
Structural highlights
FunctionFCGR1_HUMAN High affinity receptor for the Fc region of immunoglobulins gamma. Functions in both innate and adaptive immune responses.[1] [2] [3] [4] Publication Abstract from PubMedThe three-dimensional structure of a human IgG1 Fc fragment bound to wild-type human FcgammaRI is reported. The structure of the corresponding complex was solved at a resolution of 2.4 A using molecular replacement; this is the highest resolution achieved for an unmutated FcgammaRI molecule. This study highlights the critical structural and functional role played by the second extracellular subdomain of FcgammaRI. It also explains the long-known major energetic contribution of the Fc `LLGG' motif at positions 234-237, and particularly of Leu235, via a `lock-and-key' mechanism. Finally, a previously held belief is corrected and a differing view is offered on the recently proposed direct role of Fc carbohydrates in the corresponding interaction. Structural evidence is provided that such glycan-related effects are strictly indirect. Structural insights into the interaction of human IgG1 with FcgammaRI: no direct role of glycans in binding.,Oganesyan V, Mazor Y, Yang C, Cook KE, Woods RM, Ferguson A, Bowen MA, Martin T, Zhu J, Wu H, Dall'Acqua WF Acta Crystallogr D Biol Crystallogr. 2015 Nov 1;71(Pt 11):2354-61. doi:, 10.1107/S1399004715018015. Epub 2015 Oct 31. PMID:26527150[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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