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Domain‐Swapping Design by Polyproline Rod Insertion
Author(s) -
Shiga Shota,
Yamanaka Masaru,
Fujiwara Wataru,
Hirota Shun,
Goda Shuichiro,
Makabe Koki
Publication year - 2019
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201900179
Subject(s) - polyproline helix , chemistry , oligomer , domain (mathematical analysis) , dimer , crystallography , peptide , biochemistry , mathematics , organic chemistry , mathematical analysis
During domain swapping, proteins mutually interconvert structural elements to form a di‐/oligomer. Engineering this process by design is important for creating a higher order protein assembly with minimal modification. Herein, a simple design strategy is shown for domain‐swapping formation by loop deletion and insertion of a polyproline rod. Crystal structures revealed the formation of the domain‐swapped dimers and polyproline portion formed a polyproline II (PPII) structure. Small‐angle X‐ray scattering demonstrated that an extended orientation of domain‐swapped dimer was retained in solution. It is 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.