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Journal of Virology, February 2002, p. 1876-1883, Vol. 76, No. 4
0022-538X/01/$04.00+0 DOI: 10.1128/JVI.76.4.1876-1883.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.
Oleg Iourin,1,2 Zihe Rao,3 Elizabeth Fry,1 Alan Kingsman,2,
and David I. Stuart1,4*
Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN,1 Department of Biochemistry, University of Oxford, Oxford OX1 3QU,,2 Oxford Centre for Molecular Sciences, University of Oxford, Oxford OX1 3QT, United Kingdom,4 Laboratory of Structural Biology, School of Life Science and Engineering, Tsinghua University, Beijing 100084, People's Republic of China3
Received 23 July 2001/ Accepted 6 November 2001
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-Å 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.
Present address: Protein Research Group, RIKEN Genomic Sciences Center, Tsurumi, Yokohama 230-0045, Japan.
Oxford BioMedica, Oxford OX4 4GA, United Kingdom.
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