Oligomerization of the carboxyl terminal domain of the human coronavirus 229E nucleocapsid protein. Issue 2 (22nd November 2012)

• Record Type: Journal Article
• Authors: Lo, Yu-Sheng; Lin, Shing-Yen; Wang, Shiu-Mei; Wang, Chin-Tien; Chiu, Ya-Li; Huang, Tai-Huang; Hou, Ming-Hon
• Is Part Of: FEBS letters. Volume 587:Issue 2(2013)
• Page Start: 120
• Page End: 127
• Publication Date: 2012-11-22
• Subjects: HCoV -- human coronavirus -- CoV -- coronavirus -- RNP -- ribonucleoprotein -- N protein -- nucleocapsid protein -- S -- spike -- M -- membrane -- E -- envelope -- Tm -- melting temperature -- SR-rich -- serine–arginine-rich -- IBV -- avian infectious bronchitis virus -- SARS -- severe acute respiratory syndrome -- MHV -- murine hepatitis virus -- SDS -- sodium dodecyl sulfate -- Human coronavirus -- 229E strain -- Nucleocapsid protein -- Ribonucleocapsid -- C-terminal domain -- Oligomerization -- Secondary structure -- Stability; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2012.11.016
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : N and N bind by cross‐linking study (View Interaction: 1, 2, 3, 4) Abstract : ► The role of the C‐terminal tail of the HCoV‐229E N protein in oligomerization. ► A correlation between oligomerization and thermostability. ► The C‐terminal tail peptide interferes with the oligomerization. ► The development of drugs to disrupt the oligomerization of the viral N protein.