Fig. 5
From: A five-residue motif for the design of domain swapping in proteins
Domain swapping in MK-Ctd. a Structure of the C-terminal domain of the hyperthermophilic protein MK0293 (MK-Ctd) (PDB ID: 3C19) is shown. Different secondary structural elements, the N-termini and C-termini, and loop1, loop2, and loop3 of MK-Ctd are indicated. b Size exclusion profiles of MK-Ctd, L1MK-Ctd, L1MK-Ctd*, and L1MK-Ctd**, at pH 8, are shown. L1MK-Ctd* and L1MK-Ctd** are variants of L1MK-Ctd, in which the QVVAG sequence was mutated to QVNAG and QNNAG, respectively. Elution volumes corresponding to the monomeric and dimeric species are indicated. c An overlay of the 15N-HSQC spectra of the monomeric wt MK-Ctd (blue) and the dimeric L1MK-Ctd (red) is shown. d CSP between MK-Ctd and L1MK-Ctd is shown for each residue. A weighted chemical shift difference (1H and 15N) is plotted. For reference, the secondary structural arrangement of MK-Ctd is indicated on the top. e Ribbon representation of the solution dimer of L1MK-Ctd is shown. The two polypeptide chains contributing to the swapped dimer are colored in orange and purple. f A space-filling model of the L1MK-Ctd domain-swapped dimer is shown to highlight the quaternary arrangement of the protomers. Source data are provided as a Source Data file
