1bog
From Proteopedia
(New page: 200px<br /> <applet load="1bog" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bog, resolution 2.6Å" /> '''ANTI-P24 (HIV-1) FAB...) |
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| - | [[Image:1bog.gif|left|200px]]<br /> | + | [[Image:1bog.gif|left|200px]]<br /><applet load="1bog" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1bog" size=" | + | |
caption="1bog, resolution 2.6Å" /> | caption="1bog, resolution 2.6Å" /> | ||
'''ANTI-P24 (HIV-1) FAB FRAGMENT CB41 COMPLEXED WITH AN EPITOPE-HOMOLOGOUS PEPTIDE'''<br /> | '''ANTI-P24 (HIV-1) FAB FRAGMENT CB41 COMPLEXED WITH AN EPITOPE-HOMOLOGOUS PEPTIDE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The X-ray crystal structures of an anti-p24 (HIV-1) monoclonal antibody | + | The X-ray crystal structures of an anti-p24 (HIV-1) monoclonal antibody Fab fragment alone and in complexes with the epitope peptide GATPQDLNTnL (n = norleucine), an epitope-homologous peptide GATPEDLNQKLAGN, as well as two unrelated peptides GLYEWGGARITNTD and efslkGpllqwrsG (D-peptide), are presented to a maximum resolution of 2.6 A. The latter three peptides were identified from screening synthetic combinatorial peptide libraries. Although all peptides bind to the same antigen combining site, the nonhomologous peptides adopt different binding conformations and also form their critical contacts with different antibody residues. Only small readjustments are observed within the framework of the Fab fragment upon binding. |
==About this Structure== | ==About this Structure== | ||
| - | 1BOG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1BOG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BOG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: polyspecificity]] | [[Category: polyspecificity]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:57:23 2008'' |
Revision as of 09:57, 21 February 2008
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ANTI-P24 (HIV-1) FAB FRAGMENT CB41 COMPLEXED WITH AN EPITOPE-HOMOLOGOUS PEPTIDE
Overview
The X-ray crystal structures of an anti-p24 (HIV-1) monoclonal antibody Fab fragment alone and in complexes with the epitope peptide GATPQDLNTnL (n = norleucine), an epitope-homologous peptide GATPEDLNQKLAGN, as well as two unrelated peptides GLYEWGGARITNTD and efslkGpllqwrsG (D-peptide), are presented to a maximum resolution of 2.6 A. The latter three peptides were identified from screening synthetic combinatorial peptide libraries. Although all peptides bind to the same antigen combining site, the nonhomologous peptides adopt different binding conformations and also form their critical contacts with different antibody residues. Only small readjustments are observed within the framework of the Fab fragment upon binding.
About this Structure
1BOG is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Crystallographic analysis of anti-p24 (HIV-1) monoclonal antibody cross-reactivity and polyspecificity., Keitel T, Kramer A, Wessner H, Scholz C, Schneider-Mergener J, Hohne W, Cell. 1997 Dec 12;91(6):811-20. PMID:9413990
Page seeded by OCA on Thu Feb 21 11:57:23 2008
