2dts
From Proteopedia
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|PDB= 2dts |SIZE=350|CAPTION= <scene name='initialview01'>2dts</scene>, resolution 2.20Å | |PDB= 2dts |SIZE=350|CAPTION= <scene name='initialview01'>2dts</scene>, resolution 2.20Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | + | |LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= IGHG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= IGHG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1h3x|1H3X]], [[1e4k|1E4K]], [[1t83|1T83]], [[1l6x|1L6X]], [[1hzh|1HZH]], [[2dtq|2DTQ]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dts OCA], [http://www.ebi.ac.uk/pdbsum/2dts PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2dts RCSB]</span> | ||
}} | }} | ||
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[[Category: Shitara, K.]] | [[Category: Shitara, K.]] | ||
[[Category: Yamaguchi, Y.]] | [[Category: Yamaguchi, Y.]] | ||
| - | [[Category: NAG]] | ||
[[Category: defucosylated glycoform]] | [[Category: defucosylated glycoform]] | ||
[[Category: igg1]] | [[Category: igg1]] | ||
[[Category: immunoglobulin]] | [[Category: immunoglobulin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:39:21 2008'' |
Revision as of 23:39, 30 March 2008
| |||||||
| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | IGHG1 (Homo sapiens) | ||||||
| Related: | 1H3X, 1E4K, 1T83, 1L6X, 1HZH, 2DTQ
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of the Defucosylated Fc Fragment from Human Immunoglobulin G1
Overview
Removal of the fucose residue from the oligosaccharides attached to Asn297 of human immunoglobulin G1 (IgG1) results in a significant enhancement of antibody-dependent cellular cytotoxicity (ADCC) via improved IgG1 binding to Fcgamma receptor IIIa. To provide structural insight into the mechanisms of affinity enhancement, we determined the crystal structure of the nonfucosylated Fc fragment and compared it with that of fucosylated Fc. The overall conformations of the fucosylated and nonfucosylated Fc fragments were similar except for hydration mode around Tyr296. Stable-isotope-assisted NMR analyses confirmed the similarity of the overall structures between fucosylated and nonfucosylated Fc fragments in solution. These data suggest that the glycoform-dependent ADCC enhancement is attributed to a subtle conformational alteration in a limited region of IgG1-Fc. Furthermore, the electron density maps revealed that the traces between Asp280 and Asn297 of our fucosylated and nonfucosylated Fc crystals were both different from that in previously reported isomorphous Fc crystals.
About this Structure
2DTS is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural comparison of fucosylated and nonfucosylated Fc fragments of human immunoglobulin G1., Matsumiya S, Yamaguchi Y, Saito J, Nagano M, Sasakawa H, Otaki S, Satoh M, Shitara K, Kato K, J Mol Biol. 2007 May 4;368(3):767-79. Epub 2007 Feb 22. PMID:17368483
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