1cft: Difference between revisions

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==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.

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==

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[[Category: polyspecificity]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri~~ Feb ~~15 15~~:35:40 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:05:41 2008''

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 25: / Line 25: @@
 [[Category: polyspecificity]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:35:40 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:05:41 2008''