Journal article
Crystal structure of the hinge domain of Smchd1 reveals its dimerization mode and nucleic acid–binding residues
K Chen, RW Birkinshaw, AD Gurzau, I Wanigasuriya, R Wang, M Iminitoff, JJ Sandow, SN Young, PJ Hennessy, TA Willson, DA Heckmann, AI Webb, ME Blewitt, PE Czabotar, JM Murphy
Science Signaling | AMER ASSOC ADVANCEMENT SCIENCE | Published : 2020
Abstract
Structural maintenance of chromosomes flexible hinge domain containing 1 (SMCHD1) is an epigenetic regulator in which polymorphisms cause the human developmental disorder, Bosma arhinia micropthalmia syndrome, and the degenerative disease, facioscapulohumeral muscular dystrophy. SMCHD1 is considered a noncanonical SMC family member because its hinge domain is C-terminal, because it homodimerizes rather than heterodimerizes, and because SMCHD1 contains a GHKL-type, rather than an ABC-type ATPase domain at its N terminus. The hinge domain has been previously implicated in chromatin association; however, the underlying mechanism involved and the basis for SMCHD1 homodimerization are unclear. He..
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Awarded by Australian National Health and Medical Research Council fellowships
Awarded by Australian National Health and Medical Research Council IRIISS grant
Funding Acknowledgements
This study was supported by an Australian Research Training Program scholarship (to A.D.G), a Melbourne Research Scholarship International (to I.W.), a Cancer Council Victoria fellowship (to K.C.), the Bellberry-Viertel Senior Medical Research Fellowship (to M.E.B), and Australian National Health and Medical Research Council fellowships (grant 1079700 to P.E.C.; grants 1105754 and 1172929 to J.M.M.; and grant 1098290 to P.E.C., M.E.B., and J.M.M.). Additional support was provided by the Victorian State Government Operational Infrastructure Support and the Australian National Health and Medical Research Council IRIISS grant (9000433). We thank the InSPIRE program for supporting R.W.