| Literature DB >> 31264103 |
Aaron Issaian1, Lauren Schmitt1, Alexandra Born1, Parker J Nichols1, James Sikela1, Kirk Hansen1, Beat Vögeli2, Morkos A Henen1,3.
Abstract
Olduvai protein domains, encoded primarily by NBPF genes, have been linked to both human brain evolution and cognitive diseases such as autism and schizophrenia. There are six primary domains that comprise the Olduvai family: three conserved domains (CON1-3) and three human lineage-specific domains (HLS1-3), which typically occur as a triplet (HLS1, HLS2 and HLS3). Herein, we present the solution NMR assignment of the backbone chemical shifts of the separate HLS1, 2 and 3 domains of NBPF15. Our data suggest that there is no change in the structure of the separate domains when compared to the full-length triplet (HLS1-HLS2-HLS3). We also demonstrate that there is no direct interaction between the three domains.Entities:
Keywords: Autism; Backbone chemical shift assignment; Brain evolution; DUF1220; Gene duplication; Olduvai; Protein domains; Schizophrenia
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Year: 2019 PMID: 31264103 PMCID: PMC6715528 DOI: 10.1007/s12104-019-09902-0
Source DB: PubMed Journal: Biomol NMR Assign ISSN: 1874-270X Impact factor: 0.746