Structure of an Fab Fragment against a C-terminal Peptide of hCG at 2.0 Å Resolution
| Autor: | E Bos, Annemarie deHaan, Paul Emsley, Wim J.G. Schielen, Constantina Fotinou, Neil W. Isaacs, Jeremy Beauchamp |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
Protein Conformation
medicine.drug_class Stereochemistry Molecular Sequence Data Peptide Immunoglobulin domain Crystallography X-Ray Monoclonal antibody Chorionic Gonadotropin Biochemistry Cell Line Epitopes Immunoglobulin Fab Fragments medicine Humans Molecular replacement Amino Acid Sequence Molecular Biology chemistry.chemical_classification Sequence Homology Amino Acid Linear epitope biology Chemistry Hydrogen Bonding Cell Biology computer.file_format Protein Data Bank Peptide Fragments biology.protein Antibody computer Hapten |
| Zdroj: | Journal of Biological Chemistry. 273:22515-22518 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.273.35.22515 |
| Popis: | 3A2 is an antibody raised against human chorionic gonadotropin and recognizes a linear epitope on the C-terminal peptide of the human chorionic gonadotropin β-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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|