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'''CRYSTAL STRUCTURE OF AN ANTI-HCG FAB''' | '''CRYSTAL STRUCTURE OF AN ANTI-HCG FAB''' | ||
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[[Category: Isaacs, N W.]] | [[Category: Isaacs, N W.]] | ||
[[Category: Schielen, W J.G.]] | [[Category: Schielen, W J.G.]] | ||
[[Category: | [[Category: Fab-fragment]] | ||
[[Category: | [[Category: Monoclonal antibody]] | ||
[[Category: | [[Category: Reproduction]] | ||
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Revision as of 05:31, 3 May 2008
CRYSTAL STRUCTURE OF AN ANTI-HCG FAB
Overview
3A2 is an antibody raised against human chorionic gonadotropin and recognizes a linear epitope on the C-terminal peptide of the human chorionic gonadotropin beta-subunit. Its three-dimensional structure has been determined to 2-A resolution using molecular replacement and refined to a conventional R-factor of 18.2%. The protein exhibits the typical immunoglobulin fold, and the model contains 944 ordered water molecules and one sulfate ion. A comparison of the complementarity-determining regions of the Fab3A2 with those from the Protein Data Bank following the canonical structure method reveals a canonical main chain conformation. This antibody belongs to the canonical structure class (combination of canonical conformations of the complementarity determining loops) that shows a preference for haptens and not for peptides. However, the shape of the surface of the antigen binding loops resembles that of an anti-peptide antibody.
About this Structure
1SBS is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structure of an Fab fragment against a C-terminal peptide of hCG at 2.0 A resolution., Fotinou C, Beauchamp J, Emsley P, deHaan A, Schielen WJ, Bos E, Isaacs NW, J Biol Chem. 1998 Aug 28;273(35):22515-8. PMID:9712877 Page seeded by OCA on Sat May 3 08:31:23 2008
