The dimer interface of the SARS coronavirus nucleocapsid protein adapts a porcine respiratory and reproductive syndrome virus-like structure

FEBS Letters

Volumn 579, Issue 25, 2005, Pages 5663-5668

  Chang, Chung Ke ^a   Sue, Shih Che ^a   Yu, Tsan Hung ^a   Hsieh, Chiu Min ^a   Tsai, Cheng Kun ^a,c   Chiang, Yen Chieh ^a   Lee, Shin Jye ^a   Hsiao, Hsin Hao ^a   Wu, Wen Jin ^a   Chang, Chi Fon ^b   Huang, Tai Huang ^a,b,c  

^a INSTITUTE OF BIOMEDICAL SCIENCES   (Taiwan)

^b GENOMICS RESEARCH CENTER   (Taiwan)

^c NATIONAL TAIWAN NORMAL UNIVERSITY   (Taiwan)

Author keywords

Capsid protein; Coronavirus; NMR; Oligomerization; SARS

Indexed keywords

NUCLEOCAPSID PROTEIN; VIRUS PROTEIN;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTERIVIRUS; ARTICLE; BETA SHEET; CORONAVIRUS; DIMERIZATION; HYDROGEN BOND; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN STRUCTURE; SARS CORONAVIRUS; SEQUENCE ALIGNMENT;

AMINO ACID SEQUENCE; ANIMALS; DIMERIZATION; HYDROGEN BONDING; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; NUCLEOCAPSID PROTEINS; PORCINE RESPIRATORY AND REPRODUCTIVE SYNDROME VIRUS; PROTEIN STRUCTURE, SECONDARY; SARS VIRUS; SEQUENCE ALIGNMENT;

ARTERIVIRUS; CORONAVIRUS; MIRIDAE; PORCINE REPRODUCTIVE AND RESPIRATORY SYNDROME VIRUS; SARS CORONAVIRUS;

EID: 26844453741     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2005.09.038     Document Type: Article

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