1sbs

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(New page: 200px<br /> <applet load="1sbs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sbs, resolution 2.0&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 07:35, 18 November 2007


1sbs, resolution 2.0Å

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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 with SO4 as ligand. 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

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