5H2B

Structure of a novel antibody G196

Summary for 5H2B

• Entry DOI: 10.2210/pdb5h2b/pdb
• Descriptor: G196 antibody Heavy chain, G196 antibody Light chain (3 entities in total)
• Functional Keywords: antibody, immune system
• Biological source: Mus musculus; More
• Total number of polymer chains: 2
• Total formula weight: 47263.56

Authors

Park, S.Y.,Sugiyama, K. (deposition date: 2016-10-14, release date: 2017-03-22, Last modification date: 2024-10-16)

Primary citation

Tatsumi, K.,Sakashita, G.,Nariai, Y.,Okazaki, K.,Kato, H.,Obayashi, E.,Yoshida, H.,Sugiyama, K.,Park, S.Y.,Sekine, J.,Urano, T.
G196 epitope tag system: a novel monoclonal antibody, G196, recognizes the small, soluble peptide DLVPR with high affinity.
Sci Rep, 7:43480-43480, 2017

PubMed Abstract: The recognition specificity of monoclonal antibodies (mAbs) has made mAbs among the most frequently used tools in both basic science research and in clinical diagnosis and therapies. Precise determination of the epitope allows the development of epitope tag systems to be used with recombinant proteins for various purposes. Here we describe a new family of tag derived from the epitope recognized by a highly specific mAb G196. The minimal epitope was identified as the five amino acid sequence Asp-Leu-Val-Pro-Arg. Permutation analysis was used to characterize the binding requirements of mAb G196, and the variable regions of the mAb G196 were identified and structurally analyzed by X-ray crystallography. Isothermal titration calorimetry revealed the high affinity (K = 1.25 nM) of the mAb G196/G196-epitope peptide interaction, and G196-tag was used to detect several recombinant cytosolic and nuclear proteins in human and yeast cells. mAb G196 is valuable for developing a new peptide tagging system for cell biology and biochemistry research.

PubMed: 28266535
DOI: 10.1038/srep43480

Experimental method

X-RAY DIFFRACTION (2.001 Å)