Solution NMR backbone assignment reveals interaction-free tumbling of human lineage-specific Olduvai protein domains
| Autor: | Parker J. Nichols, Kirk C. Hansen, Morkos A. Henen, James M. Sikela, Alexandra Born, Lauren R. Schmitt, Aaron Issaian, Beat Vögeli |
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| Rok vydání: | 2019 |
| Předmět: |
0303 health sciences
Schizophrenia (object-oriented programming) 030303 biophysics Protein domain Intracellular Signaling Peptides and Proteins Computational biology Human brain Biology medicine.disease Biochemistry DUF1220 Article Solutions 03 medical and health sciences Lineage specific medicine.anatomical_structure Protein Domains Structural Biology Gene duplication medicine Autism Humans Gene Nuclear Magnetic Resonance Biomolecular 030304 developmental biology |
| Zdroj: | Biomol NMR Assign |
| ISSN: | 1874-270X |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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