Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 12, Issue 6, Pages 526-532Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb937
Keywords
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Funding
- NIAID NIH HHS [AI37581, AI62249, AI39394] Funding Source: Medline
- NIGMS NIH HHS [GM47467, P01 GM047467] Funding Source: Medline
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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.
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