1dqd
From Proteopedia
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'''CRYSTAL STRUCTURE OF FAB HGR-2 F6, A COMPETITIVE ANTAGONIST OF THE GLUCAGON RECEPTOR''' | '''CRYSTAL STRUCTURE OF FAB HGR-2 F6, A COMPETITIVE ANTAGONIST OF THE GLUCAGON RECEPTOR''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DQD OCA]. | |
==Reference== | ==Reference== | ||
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:[http://www.ncbi.nlm.nih.gov/pubmed/10771426 10771426] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10771426 10771426] | ||
| - | [[Category: Mus musculus]] | ||
| - | [[Category: Protein complex]] | ||
[[Category: Brzozowski, A M.]] | [[Category: Brzozowski, A M.]] | ||
[[Category: Bywater, R P.]] | [[Category: Bywater, R P.]] | ||
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[[Category: Vissing, H.]] | [[Category: Vissing, H.]] | ||
[[Category: Wright, L M.]] | [[Category: Wright, L M.]] | ||
| - | [[Category: | + | [[Category: Antigen binding site]] |
| - | [[Category: | + | [[Category: Complementarity-determining region]] |
| - | [[Category: | + | [[Category: Fab]] |
| - | [[Category: | + | [[Category: Glucagon receptor]] |
| - | [[Category: | + | [[Category: Heavy chain]] |
| - | [[Category: | + | [[Category: Light chain]] |
| - | [[Category: | + | [[Category: Monoclonal antibody]] |
| - | [[Category: | + | [[Category: Receptor antagonist]] |
| - | [[Category: | + | [[Category: Typical immunoglobulin fold]] |
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Revision as of 11:09, 2 May 2008
CRYSTAL STRUCTURE OF FAB HGR-2 F6, A COMPETITIVE ANTAGONIST OF THE GLUCAGON RECEPTOR
Overview
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 Structure
Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 14:09:00 2008
Categories: Brzozowski, A M. | Bywater, R P. | Hubbard, R E. | Pike, A C.W. | Roberts, S M. | Skovgaard, R N. | Svendsen, I. | Vissing, H. | Wright, L M. | Antigen binding site | Complementarity-determining region | Fab | Glucagon receptor | Heavy chain | Light chain | Monoclonal antibody | Receptor antagonist | Typical immunoglobulin fold
