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From Proteopedia
Loop deletion mutant (deleting two residues)
Structural highlights
Publication Abstract from PubMedIn "domain-swapping," proteins mutually interconvert structural elements to form a dimer/oligomer. Engineering this process by design is important for creating a higher order protein assembly with minimal modification. Herein, we show a simple design strategy for domain-swapping formation by loop deletion and insertion of a polyproline rod. Crystal structures revealed the formation of the domain-swapped dimers and the polyproline portion formed a polyproline II (PPII) structure. Small-angle x-ray scattering (SAXS) demonstrated that an extended orientation of domain-swapped dimer was retained in the solution. We found that a multiple of three of inserting proline residue is favored for domain-swapping because of the helical nature of PPII. The rigid nature of the polyproline rod enables precise control of the interdomain distance and orientation. Domain-swapping design by poly-proline rod insertion.,Shiga S, Yamanaka M, Fujiwara W, Hirota S, Goda S, Makabe K Chembiochem. 2019 May 15. doi: 10.1002/cbic.201900179. PMID:31094059[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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