Your browser doesn't support javascript.
The Inherent Dynamics and Interaction Sites of the SARS-CoV-2 Nucleocapsid N-Terminal Region.
Redzic, Jasmina S; Lee, Eunjeong; Born, Alexandra; Issaian, Aaron; Henen, Morkos A; Nichols, Parker J; Blue, Ashley; Hansen, Kirk C; D'Alessandro, Angelo; Vögeli, Beat; Eisenmesser, Elan Zohar.
  • Redzic JS; Department of Biochemistry and Molecular Genetics, School of Medicine, University of Colorado Denver, School of Medicine, Aurora, CO 80045, United States.
  • Lee E; Department of Biochemistry and Molecular Genetics, School of Medicine, University of Colorado Denver, School of Medicine, Aurora, CO 80045, United States.
  • Born A; Department of Biochemistry and Molecular Genetics, School of Medicine, University of Colorado Denver, School of Medicine, Aurora, CO 80045, United States.
  • Issaian A; Department of Biochemistry and Molecular Genetics, School of Medicine, University of Colorado Denver, School of Medicine, Aurora, CO 80045, United States.
  • Henen MA; Department of Biochemistry and Molecular Genetics, School of Medicine, University of Colorado Denver, School of Medicine, Aurora, CO 80045, United States; Faculty of Pharmacy, Mansoura University, Mansoura 35516, Egypt.
  • Nichols PJ; Department of Biochemistry and Molecular Genetics, School of Medicine, University of Colorado Denver, School of Medicine, Aurora, CO 80045, United States.
  • Blue A; National High Magnetic Field Laboratory, Tallahassee, FL 32310, United States.
  • Hansen KC; Department of Biochemistry and Molecular Genetics, School of Medicine, University of Colorado Denver, School of Medicine, Aurora, CO 80045, United States.
  • D'Alessandro A; Department of Biochemistry and Molecular Genetics, School of Medicine, University of Colorado Denver, School of Medicine, Aurora, CO 80045, United States.
  • Vögeli B; Department of Biochemistry and Molecular Genetics, School of Medicine, University of Colorado Denver, School of Medicine, Aurora, CO 80045, United States. Electronic address: beat.vogeli@cuanschutz.edu.
  • Eisenmesser EZ; Department of Biochemistry and Molecular Genetics, School of Medicine, University of Colorado Denver, School of Medicine, Aurora, CO 80045, United States. Electronic address: Elan.Eisenmesser@ucdenver.edu.
J Mol Biol ; 433(15): 167108, 2021 07 23.
Article in English | MEDLINE | ID: covidwho-1275497
ABSTRACT
The nucleocapsid protein is one of four structural proteins encoded by SARS-CoV-2 and plays a central role in packaging viral RNA and manipulating the host cell machinery, yet its dynamic behavior and promiscuity in nucleotide binding has made standard structural methods to address its atomic-resolution details difficult. To begin addressing the SARS-CoV-2 nucleocapsid protein interactions with both RNA and the host cell along with its dynamic behavior, we have specifically focused on the folded N-terminal domain (NTD) and its flanking regions using nuclear magnetic resonance solution studies. Studies performed here reveal a large repertoire of interactions, which includes a temperature-dependent self-association mediated by the disordered flanking regions that also serve as binding sites for host cell cyclophilin-A while nucleotide binding is largely mediated by the central NTD core. NMR studies that include relaxation experiments have revealed the complicated dynamic nature of this viral protein. Specifically, while much of the N-terminal core domain exhibits micro-millisecond motions, a central ß-hairpin shows elevated inherent flexibility on the pico-nanosecond timescale and the serine/arginine-rich region of residues 176-209 undergoes multiple exchange phenomena. Collectively, these studies have begun to reveal the complexities of the nucleocapsid protein dynamics and its preferred interaction sites with its biological targets.
Subject(s)
Keywords

Full text: Available Collection: International databases Database: MEDLINE Main subject: Spike Glycoprotein, Coronavirus / Angiotensin-Converting Enzyme 2 / SARS-CoV-2 / Mutation Limits: Humans Language: English Journal: J Mol Biol Year: 2021 Document Type: Article Affiliation country: J.jmb.2021.167108

Similar

MEDLINE

...
LILACS

LIS


Full text: Available Collection: International databases Database: MEDLINE Main subject: Spike Glycoprotein, Coronavirus / Angiotensin-Converting Enzyme 2 / SARS-CoV-2 / Mutation Limits: Humans Language: English Journal: J Mol Biol Year: 2021 Document Type: Article Affiliation country: J.jmb.2021.167108