9MCY
CRYSTAL STRUCTURE OF HUMAN IGG1 FC FRAGMENT-FC-GAMMA RECEPTOR IIA COMPLEX R131 VARIANT
Summary for 9MCY
| Entry DOI | 10.2210/pdb9mcy/pdb |
| Descriptor | Immunoglobulin gamma-1 heavy chain Fc fragment, Fc gamma receptor IIA R131 variant, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total) |
| Functional Keywords | immunoglobulin, igg1, immune system, immunoglobulin-like beta sandwich, fc fragment, fc gamma receptor iia, cd32a |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 6 |
| Total formula weight | 146205.74 |
| Authors | Tolbert, W.D.,Pazgier, M. (deposition date: 2024-12-05, release date: 2025-12-03, Last modification date: 2026-01-07) |
| Primary citation | Tolbert, W.D.,Nhan, P.B.,Conley, H.E.,Ge, X.,Chandravanshi, M.,Lee, M.,Veilleux, J.,Korzeniowski, M.,Gottumukkala, S.,Ackerman, M.E.,Pollara, J.,Pazgier, M. Cross-species analysis of Fc gamma RIIa/b (CD32a/b) polymorphisms at position 131: structural and functional insights into the mechanism of IgG- mediated phagocytosis in human and macaque. Front Immunol, 16:1726068-1726068, 2025 Cited by PubMed Abstract: Antibodies play a critical role in immunity in part by mediating clearance of pathogens and infected cells by antibody-dependent cellular phagocytosis (ADCP) through engagement of Fc gamma receptors (FcγRs) on innate immune cells. Among these, FcγRIIa (CD32a) is a key activating receptor expressed on macrophages, dendritic cells, and other antigen-presenting cells. Its affinity for IgG and ability to mediate ADCP is influenced by allelic polymorphisms. In humans, a single amino acid polymorphism at position 131, where histidine (H) is substituted with arginine (R), leads to decreased IgG1 and IgG2 subclass binding affinity and, consequently, lower efficiency of phagocytic responses. Rhesus macaques (), which are widely used as nonhuman primate models, exhibit a similar polymorphism at position 131 of FcγRIIa, but with arginine replaced by proline (P). Here, we investigated structure-function relationships associated with the FcγRIIa polymorphism at position 131 in both species, specifically with respect to IgG1 and IgG2. PubMed: 41445744DOI: 10.3389/fimmu.2025.1726068 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.85 Å) |
Structure validation
Download full validation report
