2ZPK
Crystal structure of P20.1 Fab fragment in complex with its antigen peptide
Summary for 2ZPK
| Entry DOI | 10.2210/pdb2zpk/pdb |
| Descriptor | IgG1-lambda P20.1 Fab (light chain), IgG1-lambda P20.1 Fab (heavy chain), Proteinase-activated receptor 4, ... (5 entities in total) |
| Functional Keywords | mouse igg fab fragment in complex with antigen peptide, immune system |
| Biological source | Mus musculus (mouse) More |
| Total number of polymer chains | 6 |
| Total formula weight | 94371.76 |
| Authors | Nogi, T.,Sanagawa, T.,Takagi, J. (deposition date: 2008-07-16, release date: 2008-12-23, Last modification date: 2024-11-20) |
| Primary citation | Nogi, T.,Sangawa, T.,Tabata, S.,Nagae, M.,Tamura-Kawakami, K.,Beppu, A.,Hattori, M.,Yasui, N.,Takagi, J. Novel affinity tag system using structurally defined antibody-tag interaction: application to single-step protein purification Protein Sci., 17:2120-2126, 2008 Cited by PubMed Abstract: Biologically important human proteins often require mammalian cell expression for structural studies, presenting technical and economical problems in the production/purification processes. We introduce a novel affinity peptide tagging system that uses a low affinity anti-peptide monoclonal antibody. Concatenation of the short recognition sequence enabled the successful engineering of an 18-residue affinity tag with ideal solution binding kinetics, providing a low-cost purification means when combined with nondenaturing elution by water-miscible organic solvents. Three-dimensional information provides a firm structural basis for the antibody-peptide interaction, opening opportunities for further improvements/modifications. PubMed: 18787202DOI: 10.1110/ps.038299.108 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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