1Z9E

Solution structure of the HIV-1 integrase-binding domain in LEDGF/p75

Summary for 1Z9E

• Entry DOI: 10.2210/pdb1z9e/pdb
• Descriptor: PC4 and SFRS1 interacting protein 2 (1 entity in total)
• Functional Keywords: heat repeat-like, ledgf, protein binding-transcription complex, protein binding/transcription
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: O75475
• Total number of polymer chains: 1
• Total formula weight: 14628.92

Authors

Cherepanov, P.,Sun, Z.-Y.J.,Rahman, S.,Maertens, G.,Wagner, G.,Engelman, A. (deposition date: 2005-04-01, release date: 2005-05-17, Last modification date: 2024-05-22)

Primary citation

Cherepanov, P.,Sun, Z.-Y.J.,Rahman, S.,Maertens, G.,Wagner, G.,Engelman, A.
Solution structure of the HIV-1 integrase-binding domain in LEDGF/p75
Nat.Struct.Mol.Biol., 12:526-532, 2005

PubMed Abstract: Lens epithelium-derived growth factor (LEDGF)/p75 is the dominant binding partner of HIV-1 integrase (IN) in human cells. We have determined the NMR structure of the integrase-binding domain (IBD) in LEDGF and identified amino acid residues essential for the interaction. The IBD is a compact right-handed bundle composed of five alpha-helices. Based on folding topology, the IBD is structurally related to a diverse family of alpha-helical proteins that includes eukaryotic translation initiation factor eIF4G and karyopherin-beta. LEDGF residues essential for the interaction with IN were localized to interhelical loop regions of the bundle structure. Interaction-defective IN mutants were previously shown to cripple replication although they retained catalytic function. The initial structure determination of a host cell factor that tightly binds to a retroviral enzyme lays the groundwork for understanding enzyme-host interactions important for viral replication.

PubMed: 15895093
DOI: 10.1038/nsmb937

Experimental method

SOLUTION NMR