1tet: Difference between revisions

Revision as of 11:45, 29 July 2008

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File:1tet.png

Template:STRUCTURE 1tet

CRYSTAL STRUCTURE OF AN ANTICHOLERA TOXIN PEPTIDE COMPLEX AT 2.3 ANGSTROMSCRYSTAL STRUCTURE OF AN ANTICHOLERA TOXIN PEPTIDE COMPLEX AT 2.3 ANGSTROMS

Template:ABSTRACT PUBMED 7690406

About this StructureAbout this Structure

1TET is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of an anticholera toxin peptide complex at 2.3 A., Shoham M, J Mol Biol. 1993 Aug 20;232(4):1169-75. PMID:7690406

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-'''CRYSTAL STRUCTURE OF AN ANTICHOLERA TOXIN PEPTIDE COMPLEX AT 2.3 ANGSTROMS'''
+===CRYSTAL STRUCTURE OF AN ANTICHOLERA TOXIN PEPTIDE COMPLEX AT 2.3 ANGSTROMS===
-==Overview==
+<!--
-Cholera toxin peptide 3 (CTP3) is a 15-residue peptide corresponding in sequence to an immunogenic loop on the surface of the B-subunits of both cholera toxin and the heat-labile toxin from Escherichia coli. TE33 is the Fab fragment of a monoclonal antibody elicited against CTP3. The crystal structure of the TE33-CTP3 complex at 2.3 A resolution reveals an antigen-binding pocket, 13 A deep and 13 A wide, which is lined with many aromatic residues. The N-terminal portion of the peptide antigen CTP3 forms a type II beta-turn that fits snugly into this pocket. At gln7 the peptide backbone of CTP3 forms a kink followed by an extended C-terminal chain that seals off the cleft and buries the beta-turn underneath it. All six complementarity-determining regions of TE33 contribute to the binding of CTP3. The antibody-peptide contacts include, in addition to van der Waals' interactions and hydrogen bonds, also one salt bridge and one water molecule, which mediates the interaction.
+The line below this paragraph, {{ABSTRACT_PUBMED_7690406}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_7690406}}
 ==About this Structure==
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 [[Category: Shoham, M.]]
 [[Category: Immunoglobulin]]
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