1dqd

File:1dqd.jpg

spinqualitylabelsall models 1dqd, resolution 2.1Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF FAB HGR-2 F6, A COMPETITIVE ANTAGONIST OF THE GLUCAGON RECEPTOR

OverviewOverview

The monoclonal antibody hGR-2 F6 has been raised against the human, glucagon receptor and shown to act as a competitive antagonist. As a first, step in the structural characterization of the receptor, the crystal, structure of the Fab fragment from this antibody is reported at 2.1 A, resolution. The hGR-2 F6 Fab crystallizes in the orthorhombic space group, P2(1)2(1)2, with unit-cell parameters a = 76.14, b = 133.74, c = 37.46 A., A model generated by homology modelling was used as an aid in the, chain-tracing and the Fab fragment structure was subsequently refined, (final R factor = 21.7%). The structure obtained exhibits the typical, immunoglobulin fold. Complementarity-determining regions (CDRs) L1, L2, L3, H1 and H2 could be superposed onto standard canonical CDR loops. The, H3 loop could be classified according to recently published rules, regarding loop length, sequence and conformation. This loop is 14 residues, long, with an approximate beta-hairpin geometry, which is distorted, somewhat by the presence of two trans proline residues at the beginning of, the loop. It is expected that this H3 loop will facilitate the design of, synthetic probes for the glucagon receptor that may be used to investigate, receptor activity.

About this StructureAbout this Structure

1DQD is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Structure of Fab hGR-2 F6, a competitive antagonist of the glucagon receptor., Wright LM, Brzozowski AM, Hubbard RE, Pike AC, Roberts SM, Skovgaard RN, Svendsen I, Vissing H, Bywater RP, Acta Crystallogr D Biol Crystallogr. 2000 May;56(Pt 5):573-80. PMID:10771426

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