Detail The Flavivirus Precursor Membrane-Envelope Protein Complex: Structure and Maturation   Oleh:  Long, Li ; Shee-Mei, Lok ; I-Mei, Yu ; Ying, Zhang Jenis: Article from Bulletin/Magazine Dalam koleksi: SCIENCE (keterangan: ada di Proquest) vol. 319 no. 5871 (Mar. 2008), page 1830-1833. Ketersediaan Perpustakaan FK Nomor Panggil: S01.K.2008.03 Non-tandon: 1 (dapat dipinjam: 0) Tandon: tidak ada     Lihat Detail Induk Isi artikel Many viruses go through a maturation step in the final stages of assembly before being transmitted to another host. The maturation process of flaviviruses is directed by the proteolytic cleavage of the precursor membrane protein (prM), turning inert virus into infectious particles. We have determined the 2.2 angstrom resolution crystal structure of a recombinant protein in which the dengue virus prM is linked to the envelope glycoprotein E. The structure represents the prM-E heterodimer and fits well into the cryo–electron microscopy density of immature virus at neutral pH. The pr peptide ß-barrel structure covers the fusion loop in E, preventing fusion with host cell membranes. The structure provides a basis for identifying the stages of its pH-directed conformational metamorphosis during maturation, ending with release of pr when budding from the host. Opini Anda Klik untuk menuliskan opini Anda tentang koleksi ini! Kembali

Copyright © 2006, 2007 Unika Atma Jaya, all rights reserved