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2d03
From Proteopedia
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|PDB= 2d03 |SIZE=350|CAPTION= <scene name='initialview01'>2d03</scene>, resolution 1.97Å | |PDB= 2d03 |SIZE=350|CAPTION= <scene name='initialview01'>2d03</scene>, resolution 1.97Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1t2q|1T2Q]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2d03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d03 OCA], [http://www.ebi.ac.uk/pdbsum/2d03 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2d03 RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Wedekind, J E.]] | [[Category: Wedekind, J E.]] | ||
[[Category: Xie, K.]] | [[Category: Xie, K.]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: MES]] | ||
| - | [[Category: PEG]] | ||
[[Category: antibody]] | [[Category: antibody]] | ||
| - | ''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 02:28:38 2008'' |
Revision as of 23:28, 30 March 2008
| |||||||
| , resolution 1.97Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Related: | 1T2Q
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the G91S mutant of the NNA7 Fab
Overview
The NNA7 Fab antibody fragment recognizes the human N-type blood-group antigen comprised of the N-terminal glycopeptide of glycophorin A (GPA). A mutant form of this Fab fragment, NNA7-G91S, exhibits markedly reduced antigen binding. To provide insight into how these Fab fragments recognize this glycopeptide antigen, the crystal structures of NNA7 and NNA7-G91S were solved and refined to 1.83 and 1.97 A resolution, respectively. Both molecules are composed of the same heavy (H) chain Fd fragment, but each contains a slightly different light (L) chain owing to the G91S substitution. Specifically, the G91S mutation pushes the backbone of the neighboring H chain away from complementarity-determining region 3 (CDR3) of the L-chain variable region, allowing an additional glycerol cryoprotectant molecule to enter the antigen-combining site near the putative location of O-linked glycosylation. Each Fab fragment also possesses a well defined 2-(N-morpholino)ethanesulfonic acid (MES) molecule trapped in its antigen-combining site, as well as a crystallographic symmetry-related molecule comprising an amino-acid sequence that is virtually identical to the N-terminus of GPA. The MES molecule interacts with the H-chain CDR in a manner reminiscent of antibody-carbohydrate complexes. These results suggest a model for recognition of the glycopeptide antigen that accounts for the deleterious effect of the G91S substitution.
About this Structure
2D03 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Crystallographic analysis of the NNA7 Fab and proposal for the mode of human blood-group recognition., Xie K, Song SC, Spitalnik SL, Wedekind JE, Acta Crystallogr D Biol Crystallogr. 2005 Oct;61(Pt 10):1386-94. Epub 2005, Sep 28. PMID:16204891
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