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| {{STRUCTURE_1zea| PDB=1zea | SCENE= }} | | {{STRUCTURE_1zea| PDB=1zea | SCENE= }} |
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| '''Structure of the anti-cholera toxin antibody Fab fragment TE33 in complex with a D-peptide'''
| | ===Structure of the anti-cholera toxin antibody Fab fragment TE33 in complex with a D-peptide=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17712773}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17712773 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17712773}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Polyspecificity]] | | [[Category: Polyspecificity]] |
| [[Category: Substitution matrix]] | | [[Category: Substitution matrix]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:31:12 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:29:25 2008'' |
