1FGL

Cyclophilin A complexed with a fragment of HIV-1 GAG protein

Summary for 1FGL

• Entry DOI: 10.2210/pdb1fgl/pdb
• Descriptor: CYCLOPHILIN A, HIV-1 GAG PROTEIN (3 entities in total)
• Functional Keywords: cyclophilin, binding protein for cyclosporin a, aids, isomerase-peptide complex, isomerase-viral protein complex, isomerase/viral protein
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm : P62937; Gag polyprotein: Host cell membrane ; Lipid-anchor . Matrix protein p17: Virion membrane ; Lipid-anchor . Capsid protein p24: Virion . Nucleocapsid protein p7: Virion : P05889
• Total number of polymer chains: 2
• Total formula weight: 20659.42

Authors

Zhao, Y.,Chen, Y.,Schutkowski, M.,Fischer, G.,Ke, H. (deposition date: 1996-11-18, release date: 1997-04-01, Last modification date: 2024-10-23)

Primary citation

Zhao, Y.,Chen, Y.,Schutkowski, M.,Fischer, G.,Ke, H.
Cyclophilin A complexed with a fragment of HIV-1 gag protein: insights into HIV-1 infectious activity.
Structure, 5:139-146, 1997

PubMed Abstract: Cyclophilin A (CyPA), a receptor of the immunosuppressive drug cyclosporin A, catalyzes the cis-trans isomerization of peptidyl-prolyl bonds and is required for the infectious activity of human immunodeficiency virus type 1 (HIV-1). The crystal structure of CyPA complexed with a fragment of the HIV-1 gag protein should provide insights into the nature of CyPA-gag interactions and may suggest a role for CyPA in HIV-1 infectious activity.

PubMed: 9016720
DOI: 10.1016/S0969-2126(97)00172-X

Experimental method

X-RAY DIFFRACTION (1.8 Å)