1zea
From Proteopedia
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|PDB= 1zea |SIZE=350|CAPTION= <scene name='initialview01'>1zea</scene>, resolution 1.78Å | |PDB= 1zea |SIZE=350|CAPTION= <scene name='initialview01'>1zea</scene>, resolution 1.78Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=CIT:CITRIC ACID'>CIT</scene> | + | |LIGAND= <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=DAS:D-ASPARTIC+ACID'>DAS</scene>, <scene name='pdbligand=DGN:D-GLUTAMINE'>DGN</scene>, <scene name='pdbligand=DHI:D-HISTIDINE'>DHI</scene>, <scene name='pdbligand=DPR:D-PROLINE'>DPR</scene>, <scene name='pdbligand=DSN:D-SERINE'>DSN</scene>, <scene name='pdbligand=DTY:D-TYROSINE'>DTY</scene>, <scene name='pdbligand=DVA:D-VALINE'>DVA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1tet|1TET]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zea OCA], [http://www.ebi.ac.uk/pdbsum/1zea PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zea RCSB]</span> | ||
}} | }} | ||
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[[Category: Seifert, M.]] | [[Category: Seifert, M.]] | ||
[[Category: Wessner, H.]] | [[Category: Wessner, H.]] | ||
- | [[Category: CIT]] | ||
[[Category: anti-cholera toxin]] | [[Category: anti-cholera toxin]] | ||
[[Category: antigen recognition]] | [[Category: antigen recognition]] | ||
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[[Category: substitution matrix]] | [[Category: substitution matrix]] | ||
- | ''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 01:34:50 2008'' |
Revision as of 22:34, 30 March 2008
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, resolution 1.78Å | |||||||
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Ligands: | , , , , , , , | ||||||
Related: | 1TET
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Structure of the anti-cholera toxin antibody Fab fragment TE33 in complex with a D-peptide
Overview
The structure of a complex of the anti-cholera toxin antibody TE33 Fab (fragment antibody) with the D-peptide vpGsqhyds was solved to 1.78 A resolution. The D-peptide was derived from the linear L-peptide epitope VPGSQHIDS by a stepwise transformation. Despite the very similar amino acid sequence-the only difference is a tyrosine residue in position 7-there are marked differences in the individual positions with respect to their contribution to the peptide overall affinity as ascertained by a complete substitutional analysis. This is reflected by the X-ray structure of the TE33 Fab/D-peptide complex where there is an inverted orientation of the D-peptide as compared with the known structure of a corresponding complex containing the epitope L-peptide, with the side chains establishing different contacts within the binding site of TE33. The D- and L-peptide affinities are comparable and the surface areas buried by complex formation are almost the same. Thus the antibody TE33 provides a typical example for polyspecific binding behavior of IgG family antibodies.
About this Structure
1ZEA is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structure of an anti-cholera toxin antibody Fab in complex with an epitope-derived D-peptide: a case of polyspecific recognition., Scheerer P, Kramer A, Otte L, Seifert M, Wessner H, Scholz C, Krauss N, Schneider-Mergener J, Hohne W, J Mol Recognit. 2007 Jul-Aug;20(4):263-74. PMID:17712773
Page seeded by OCA on Mon Mar 31 01:34:50 2008
Categories: Mus musculus | Protein complex | Hoehne, W. | Kramer, A. | Krauss, N. | Otte, L. | Scheerer, P. | Schneider-Mergener, J. | Scholz, C. | Seifert, M. | Wessner, H. | Anti-cholera toxin | Antigen recognition | Antigen-antibody complex | Cross-reactivity | Polyspecificity | Substitution matrix