8ipc

The recombinant NZ-1 Fab complexed with the PDZ tandem fragment of A. aeolicus S2P homolog with the PA14 tag inserted between the residues 181 and 184

spinqualitylabelsall models 8ipc, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8ipc is a 3 chain structure with sequence from Aquifex aeolicus VF5 and Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: PCA, SNN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Y1964_AQUAE Publication Abstract from PubMed Antigen-binding fragments (Fabs) of antibodies are both key biopharmaceuticals and valuable tools for basic life science. To streamline the production of diverse Fabs by capitalizing on standard and highly optimized protein production protocols, we here explore a method to prepare recombinant Fabs as secreted fusion proteins with an N-terminal human growth hormone domain and an octa-histidine tag. These tagged Fabs can be purified with standard immobilized metal chelate affinity chromatography. We first demonstrated Fab overproduction using the rat monoclonal antibody NZ-1. Optimization of linker residues enabled the complete removal of the tags by TEV protease, leaving only two additional residues at the N-terminus of the heavy chain. We purified NZ-1 Fab at approximately 4 mug/mL of culture supernatant and further confirmed that the NZ-1 Fab from the fusion protein maintained its native fold and binding affinity for target cell-surface antigens. We also showed that several other Fabs of mouse IgG(1)s, the major subclass in mice, could be produced with the same procedure. Our preparation method can provide greater flexibility in functional and structural modifications of target Fabs because specialized purification techniques are not necessary. Recombinant production of antibody antigen-binding fragments with an N-terminal human growth hormone tag in mammalian cells.,Adachi Y, Kaneko MK, Kato Y, Nogi T Protein Expr Purif. 2023 Aug;208-209:106289. doi: 10.1016/j.pep.2023.106289. Epub , 2023 May 7. PMID:37160213 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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