Passenger sequences can promote interlaced dimers in a common variant of the maltose-binding protein.

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 Ų. We dem

SUBMITTER: Momin AA 

PROVIDER: S-EPMC6938514 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature