ArticleScientific reports2019
Passenger sequences can promote interlaced dimers in a common variant of the maltose-binding protein.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 20 citations in OpenAlex.
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- A fusion protein designed for soluble expression, rapid purification, and enhanced stability of parasporin-2 with potential therapeutic applications.Biotechnology reports (Amsterdam, Netherlands) · 2024Article
- Autoimmune diseases: targets, biology, and drug discovery.Acta pharmacologica Sinica · 2024Review
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- PYK2 senses calcium through a disordered dimerization and calmodulin-binding element.Communications biology · 2022Article
- The exceptionally efficient quorum quenching enzyme LrsL suppressesFrontiers in microbiology · 2022Article
- Long-Lasting Stable Expression of Human LL-37 Antimicrobial Peptide in Transgenic Barley Plants.Antibiotics (Basel, Switzerland) · 2021Article
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Authors and funding
3 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The maltose-binding protein (MBP) is one of the most frequently used protein tags due to its capacity to stabilize, solubilize and even crystallize recombinant proteins that are fused to it. Given that MBP is thought to be a highly stable monomeric protein with known characteristics, fused passenger proteins are often studied without being cleaved from MBP. Here we report that a commonly used engineered MBP version (mutated to lower its surface entropy) can form interlaced dimers when fused to short protein sequences derived from the focal adhesion kinase (FAK) or the homologous protein tyrosine kinase 2 (PYK2). These MBP dimers still bind maltose and can interconvert with monomeric forms in vitro under standard conditions despite a contact surface of more than 11,000 Å
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