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The E protein is a multifunctional membrane protein of SARS-CoV / 基因组蛋白质组与生物信息学报·英文版
Genomics, Proteomics & Bioinformatics ; (4): 131-144, 2003.
Article in English | WPRIM | ID: wpr-339514
ABSTRACT
The E (envelope) protein is the smallest structural protein in all coronaviruses and is the only viral structural protein in which no variation has been detected. We conducted genome sequencing and phylogenetic analyses of SARS-CoV. Based on genome sequencing, we predicted the E protein is a transmembrane (TM) protein characterized by a TM region with strong hydrophobicity and alpha-helix conformation. We identified a segment (NH2-_L-Cys-A-Y-Cys-Cys-N_-COOH) in the carboxyl-terminal region of the E protein that appears to form three disulfide bonds with another segment of corresponding cysteines in the carboxyl-terminus of the S (spike) protein. These bonds point to a possible structural association between the E and S proteins. Our phylogenetic analyses of the E protein sequences in all published coronaviruses place SARS-CoV in an independent group in Coronaviridae and suggest a non-human animal origin.
Subject(s)
Full text: Available Index: WPRIM (Western Pacific) Main subject: Phylogeny / Protein Conformation / Codon / Membrane Glycoproteins / Molecular Sequence Data / Base Sequence / Cluster Analysis / Viral Envelope Proteins / Sequence Alignment / Amino Acid Sequence Language: English Journal: Genomics, Proteomics & Bioinformatics Year: 2003 Type: Article

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Full text: Available Index: WPRIM (Western Pacific) Main subject: Phylogeny / Protein Conformation / Codon / Membrane Glycoproteins / Molecular Sequence Data / Base Sequence / Cluster Analysis / Viral Envelope Proteins / Sequence Alignment / Amino Acid Sequence Language: English Journal: Genomics, Proteomics & Bioinformatics Year: 2003 Type: Article