4ZNE
IgG1 Fc-FcgammaRI ecd complex
Summary for 4ZNE
Entry DOI | 10.2210/pdb4zne/pdb |
Descriptor | High affinity immunoglobulin gamma Fc receptor I, Ig gamma-1 chain C region, alpha-D-mannopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total) |
Functional Keywords | antibody, constant region, receptor, high affinity, immune system |
Biological source | Homo sapiens (Human) More |
Cellular location | Cell membrane ; Single-pass type I membrane protein : P12314 Secreted: P01857 |
Total number of polymer chains | 3 |
Total formula weight | 86124.51 |
Authors | Oganesyan, V.Y.,Dall'Acqua, W.F. (deposition date: 2015-05-04, release date: 2015-11-11, Last modification date: 2024-10-30) |
Primary citation | Oganesyan, V.,Mazor, Y.,Yang, C.,Cook, K.E.,Woods, R.M.,Ferguson, A.,Bowen, M.A.,Martin, T.,Zhu, J.,Wu, H.,Dall'Acqua, W.F. Structural insights into the interaction of human IgG1 with Fc gamma RI: no direct role of glycans in binding. Acta Crystallogr.,Sect.D, 71:2354-2361, 2015 Cited by PubMed Abstract: The three-dimensional structure of a human IgG1 Fc fragment bound to wild-type human FcγRI is reported. The structure of the corresponding complex was solved at a resolution of 2.4 Å using molecular replacement; this is the highest resolution achieved for an unmutated FcγRI molecule. This study highlights the critical structural and functional role played by the second extracellular subdomain of FcγRI. 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. PubMed: 26527150DOI: 10.1107/S1399004715018015 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.42 Å) |
Structure validation
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