2WAH
Crystal Structure of an IgG1 Fc Glycoform (Man9GlcNAc2)
Summary for 2WAH
Entry DOI | 10.2210/pdb2wah/pdb |
Related | 1AJ7 1AQK 1BEY 1D5B 1D5I 1D6V 1DN2 1E4K 1FC1 1FCC 1H3T 1H3U 1H3V 1H3W 1H3Y 1I7Z 1L6X 1OQX 1T83 1T89 2IWG 2J6E 2RCS |
Descriptor | IG GAMMA-1 CHAIN C REGION, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
Functional Keywords | immunoglobulin c region, antibody engineering, immunoglobulin domain, secreted, antibody, kifunensine, glycoprotein, oligomannose, immune system, glycosylation |
Biological source | Homo sapiens (Human) |
Cellular location | Secreted : P01857 |
Total number of polymer chains | 2 |
Total formula weight | 49549.46 |
Authors | Crispin, M.,Bowden, T.A.,Coles, C.H.,Harlos, K.,Aricescu, A.R.,Harvey, D.J.,Stuart, D.I.,Jones, E.Y. (deposition date: 2009-02-06, release date: 2009-03-10, Last modification date: 2023-12-13) |
Primary citation | Crispin, M.,Bowden, T.A.,Coles, C.H.,Harlos, K.,Aricescu, A.R.,Harvey, D.J.,Stuart, D.I.,Jones, E.Y. Carbohydrate and Domain Architecture of an Immature Antibody Glycoform Exhibiting Enhanced Effector Functions J.Mol.Biol., 387:1061-, 2009 Cited by PubMed Abstract: Antibodies contain a conserved glycosylation site that has emerged as a target for the modulation of antibody effector functions. The crystal structure of a biosynthetic intermediate of human IgG1, bearing immature oligomannose-type glycans and reported to display increased antibody-dependent cellular cytotoxicity, demonstrates that glycan engineering can bias the Fc to an open conformation primed for receptor binding. PubMed: 19236877DOI: 10.1016/J.JMB.2009.02.033 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.51 Å) |
Structure validation
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