Structure of equine infectious anemia virus matrix protein.

Journal article

The Gag polyprotein is key to the budding of retroviruses from host cells and is cleaved upon virion maturation, the N-terminal membrane-binding domain forming the matrix protein (MA). The 2.8-A resolution crystal structure of MA of equine infectious anemia virus (EIAV), a lentivirus, reveals that, despite showing no sequence similarity, more than half of the molecule can be superimposed on the MAs of human immunodeficiency virus type 1 (HIV-1) and simian immunodeficiency virus (SIV). However...

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Authors: Hatanaka, H; Iourin, O; Rao, Z; Fry, E; Kingsman, A

• Publication status: Published
• Journal: Journal of virology
• Volume: 76
• Issue: 4
• Pages: 1876-1883
• Publication date: 2002-02-01
• DOI: 10.1128/jvi.76.4.1876-1883.2002
• EISSN: 1098-5514
• ISSN: 0022-538X
• Language: English
• Keywords: Viral Matrix Proteins; Viral Proteins; Models, Molecular; Crystallography, X-Ray; gag Gene Products, Human Immunodeficiency Virus; Protein Conformation; HIV Antigens; Amino Acid Sequence; Molecular Sequence Data; Crystallization; Gene Products, gag; Simian immunodeficiency virus; Infectious Anemia Virus, Equine; Sequence Alignment