1DQD

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

Summary for 1DQD

• Entry DOI: 10.2210/pdb1dqd/pdb
• Descriptor: FAB HGR-2 F6 (3 entities in total)
• Functional Keywords: glucagon receptor, monoclonal antibody, fab, receptor antagonist, typical immunoglobulin fold, light chain, heavy chain, antigen binding site, complementarity-determining regions, immune system
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 2
• Total formula weight: 47846.04

Authors

Wright, L.M.,Brzozowski, A.M.,Hubbard, R.E.,Pike, A.C.W.,Roberts, S.M.,Skovgaard, R.N.,Svendsen, I.,Vissing, H.,Bywater, R.P. (deposition date: 2000-01-04, release date: 2000-05-10, Last modification date: 2024-10-30)

Primary citation

Wright, L.M.,Brzozowski, A.M.,Hubbard, R.E.,Pike, A.C.,Roberts, S.M.,Skovgaard, R.N.,Svendsen, I.,Vissing, H.,Bywater, R.P.
Structure of Fab hGR-2 F6, a competitive antagonist of the glucagon receptor.
Acta Crystallogr.,Sect.D, 56:573-580, 2000

PubMed Abstract: 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.

PubMed: 10771426
DOI: 10.1107/S090744490000233X

Experimental method

X-RAY DIFFRACTION (2.1 Å)