Sindbis virus glycoprotein E1 is divided into two discrete domains at amino acid 129 by disulfide bridge connections.
The E1 membrane glycoprotein of Sindbis virus contains structural and functional domains, which are conformationally dependent on the presence of intramolecular disulfide bridges (B. A. Abell and D. T. Brown, J. Virol. 67:5496-5501, 1993; R. P. Anthony, A. M. Paredes, and D. T. Brown, Virology 190:330-336, 1992). We have examined the disulfide bonds in E1 and have determined that the E1 membrane glycoprotein contains two separate sets of interconnecting disulfide linkages, which divide the protein into two domains at amino acid 129. These separate sets of disulfides may stabilize and define the structural and functional regions of the E1 protein.
Phinney
B S
BS
Department of Biochemistry, North Carolina State University, Raleigh, North Carolina 27695, USA.
Brown
D T
DT
D000595:Amino Acid Sequence; D008562:Membrane Glycoproteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D012845:Sindbis Virus / Q000737:chemistry*; D013440:Sulfides; D014759:Viral Envelope Proteins / Q000737:chemistry*
D008562:Membrane Glycoproteins; D013440:Sulfides; D014759:Viral Envelope Proteins; C022012:glycoprotein E1, Sindbis virus