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New page: left|200px<br /><applet load="1tet" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tet, resolution 2.3Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1tet.gif|left|200px]]<br /><applet load="1tet" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1tet.gif|left|200px]]<br /><applet load="1tet" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1tet, resolution 2.3&Aring;" />
caption="1tet, resolution 2.3&Aring;" />
'''CRYSTAL STRUCTURE OF AN ANTICHOLERA TOXIN PEPTIDE COMPLEX AT 2.3 ANGSTROMS'''<br />
'''CRYSTAL STRUCTURE OF AN ANTICHOLERA TOXIN PEPTIDE COMPLEX AT 2.3 ANGSTROMS'''<br />


==Overview==
==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.
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.


==About this Structure==
==About this Structure==
1TET is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with CIT as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TET OCA].  
1TET is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=CIT:'>CIT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TET OCA].  


==Reference==
==Reference==
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[[Category: immunoglobulin]]
[[Category: immunoglobulin]]


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