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Publication Abstract from PubMed

Domain swapping is a process wherein a portion of a protein is exchanged with its counterpart in another copy of the molecule, resulting in the formation of homo-oligomers with concomitant repacking of a hydrophobic core. Here, we report domain swapping triggered upon modifying a beta-hairpin sequence within a single-layer beta-sheet (SLB) of a model protein, OspA that did not involve the formation of a reorganized hydrophobic core. The replacement of two beta-hairpin sequences with a Gly-Gly and shorteing of a beta-hairpin resulted in a protein that formed two distinct crystal structures under similar conditions: one was monomeric, similar to the parental molecule, whereas the other was a domain-swapped dimer, mediated by an intermolecular beta-sheet in the SLB portion. Based on the dimer interface structure, we replaced the Gly-Gly sequence with three-residue sequences that enable the formation of a consecutive intermolecular beta-sheet, including the Cys-Thr-Cys sequence that formed a stable disulfide-linked dimer. These results provide new insights into protein folding, evolution, and the designability of protein structure.

beta-Strand-mediated Domain-swapping in the Absence of Hydrophobic Core Repacking.,Kiya M, Shiga S, Ding P, Koide S, Makabe K J Mol Biol. 2024 Jan 15;436(2):168405. doi: 10.1016/j.jmb.2023.168405. Epub 2023 , Dec 15. PMID:38104859^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.