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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, unlike the structures formed by HIV-1 and SIV MAs, the oligomerization state observed is not trimeric. We discuss the potential of this molecule for membrane binding in the light of conformational differences between EIAV MA and HIV or SIV MA.

Original publication

DOI

10.1128/jvi.76.4.1876-1883.2002

Type

Journal article

Journal

J Virol

Publication Date

02/2002

Volume

76

Pages

1876 - 1883

Keywords

Amino Acid Sequence, Crystallization, Crystallography, X-Ray, Gene Products, gag, HIV Antigens, Infectious Anemia Virus, Equine, Models, Molecular, Molecular Sequence Data, Protein Conformation, Sequence Alignment, Simian Immunodeficiency Virus, Viral Matrix Proteins, Viral Proteins, gag Gene Products, Human Immunodeficiency Virus