1HEK

Crystal structure of equine infectious anaemia virus matrix antigen (EIAV MA)

Summary for 1HEK

• Entry DOI: 10.2210/pdb1hek/pdb
• Related: 1EIA 2EIA
• Descriptor: GAG POLYPROTEIN, CORE PROTEIN P15 (1 entity in total)
• Functional Keywords: viral protein, membrane-binding switching
• Biological source: EQUINE INFECTIOUS ANEMIA VIRUS (EIAV)
• Total number of polymer chains: 2
• Total formula weight: 30045.18

Authors

Hatanaka, H.,Iourin, O.,Rao, Z.,Fry, E.,Kingsman, A.,Stuart, D.I. (deposition date: 2000-11-24, release date: 2001-11-23, Last modification date: 2024-10-23)

Primary citation

Hatanaka, H.,Iourin, O.,Rao, Z.,Fry, E.,Kingsman, A.,Stuart, D.I.
Structure of Equine Infectious Anemia Virus Matrix Protein.
J.Virol., 76:1876-, 2002

PubMed Abstract: 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.

PubMed: 11799182
DOI: 10.1128/JVI.76.4.1876-1883.2002

Experimental method

X-RAY DIFFRACTION (2.8 Å)