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Structural characterizations of human periostin dimerization and cysteinylation
Author(s) -
Liu Jianmei,
Zhang Junying,
Xu Fei,
Lin Zhaohan,
Li Zhiqiang,
Liu Heli
Publication year - 2018
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13091
Subject(s) - periostin , dimer , extracellular matrix , chemistry , extracellular , microbiology and biotechnology , mutant , biophysics , biology , biochemistry , organic chemistry , gene
Human periostin plays a multifaceted role in remodeling the extracellular matrix milieu by interacting with other proteins and itself in both a heterophilic and homophilic manner. However, the structural mechanism for its extensive interactions has remained elusive. Here, we report the crystal structures of human periostin ( EMI ‐Fas1 I– IV ) and its Cys60Ala mutant. In combination with multi‐angle light‐scattering analysis and biochemical assays, the crystal structures reveal that periostin mainly exists as a dimer in solution and its homophilic interaction is mainly mediated by the EMI domain. Furthermore, Cys60 undergoes cysteinylation as confirmed by mass spectroscopy, and this site hardly affects the homophilic interaction. Also, the structures yield insights into how periostin forms heterophilic interactions with other proteins under physiological or pathological conditions.