Introducing mgTag and cTag
How do you study the 90% of proteins that lack small-molecule binding partners? By tagging the protein!
The problem is that most tags are too bulky, like trying to study a butterfly ๐ฆ with a bowling ball attached.
To address this limitation, researchers at the Broad Institute developed two novel protein tags which were published in Angewandte Chemie:
“๐๐ญ๐ต๐ณ๐ข๐ด๐ฎ๐ข๐ญ๐ญ ๐๐ฉ๐ฆ๐ฎ๐ฐ๐จ๐ฆ๐ฏ๐ฆ๐ต๐ช๐ค ๐๐ข๐จ๐ด ๐ธ๐ช๐ต๐ฉ ๐๐ณ๐ฐ๐ถ๐ฑ-๐๐ณ๐ข๐ฏ๐ด๐ง๐ฆ๐ณ ๐๐ช๐จ๐ข๐ฏ๐ฅ๐ด”
My highlights
Size:
๐ธ mgTag: 36 amino acids
๐ธ cTag: 50 amino acids
โ๏ธ Both tags use “transferase-type reactivity” (exploiting the same mechanism cells use naturally) โก๏ธ allowing attachment of any moiety-of-interest to the tag โ
โ๏ธ The mgTag operates through a molecular glue system requiring cereblon (CRBN)
โ๏ธ cTag uses an engineered C1 domain from protein kinase C
โ๏ธ The smallest covalent chemogenetic tags developed to date
โ๏ธ Both tags are of human origin: suitable for applications requiring reduced immunogenicity
This technology can find applications in basic science, proximity inducing modalities, biotechnology, and medicine, including potential use in CRISPR-based knock-in technologies and synthetic biology applications.
Share your opinion
What applications do you see for these novel protein tags โ
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Full manuscript: https://doi.org/10.1002/anie.202506997Digital Object Identifier (DOI)
