Structure of Fab hGR-2 F6, a competitive antagonist of the glucagon receptor.

作者: Lisa M. Wright , A. Marek Brzozowski , Roderick E. Hubbard , Ashley C. W. Pike , Shirley M. Roberts

DOI: 10.1107/S090744490000233X

关键词:

摘要: The monoclonal antibody hGR-2 F6 has been raised against the human glucagon receptor and shown to act as a competitive antagonist. As first step in structural characterization of receptor, crystal structure Fab fragment from this is reported at 2.1 A resolution. crystallizes orthorhombic space group P21212, with unit-cell parameters = 76.14, b = 133.74, c 37.46 A. A model generated by homology modelling was used an aid chain-tracing subsequently refined (final R factor 21.7%). obtained exhibits typical immunoglobulin fold. Complementarity-determining regions (CDRs) L1, L2, L3, H1 H2 could be superposed onto standard canonical CDR loops. H3 loop classified according recently published rules regarding length, sequence conformation. This 14 residues long, approximate β-hairpin geometry, which distorted somewhat presence two trans proline beginning loop. It expected that will facilitate design synthetic probes for may investigate activity.

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