Abstract：
: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.
journal_name
Celljournal_title
Cellauthors
Keitel T,Kramer A,Wessner H,Scholz C,Schneider-Mergener J,Höhne Wdoi
10.1016/s0092-8674(00)80469-9subject
Has Abstractpub_date
1997-12-12 00:00:00pages
811-20issue
6eissn
0092-8674issn
1097-4172pii
S0092-8674(00)80469-9journal_volume
91pub_type
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