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Open data
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Basic information
Entry | Database: PDB / ID: 7snq | ||||||
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Title | Hexamer HIV-1 CA in complex with CPSF6 peptide and IP6 ligand | ||||||
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![]() | VIRAL PROTEIN | ||||||
Function / homology | ![]() HIV-1 retropepsin / retroviral ribonuclease H / exoribonuclease H / exoribonuclease H activity / host multivesicular body / DNA integration / viral genome integration into host DNA / RNA-directed DNA polymerase / establishment of integrated proviral latency / viral penetration into host nucleus ...HIV-1 retropepsin / retroviral ribonuclease H / exoribonuclease H / exoribonuclease H activity / host multivesicular body / DNA integration / viral genome integration into host DNA / RNA-directed DNA polymerase / establishment of integrated proviral latency / viral penetration into host nucleus / RNA stem-loop binding / RNA-directed DNA polymerase activity / host cell / RNA-DNA hybrid ribonuclease activity / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / symbiont-mediated suppression of host gene expression / viral nucleocapsid / DNA recombination / DNA-directed DNA polymerase / Hydrolases; Acting on ester bonds / aspartic-type endopeptidase activity / DNA-directed DNA polymerase activity / symbiont entry into host cell / lipid binding / host cell nucleus / host cell plasma membrane / structural molecule activity / virion membrane / proteolysis / DNA binding / zinc ion binding / membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Bester, S.M. / Kvaratskhelia, M. | ||||||
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![]() | ![]() Title: Prion-like low complexity regions enable avid virus-host interactions during HIV-1 infection. Authors: Guochao Wei / Naseer Iqbal / Valentine V Courouble / Ashwanth C Francis / Parmit K Singh / Arpa Hudait / Arun S Annamalai / Stephanie Bester / Szu-Wei Huang / Nikoloz Shkriabai / Lorenzo ...Authors: Guochao Wei / Naseer Iqbal / Valentine V Courouble / Ashwanth C Francis / Parmit K Singh / Arpa Hudait / Arun S Annamalai / Stephanie Bester / Szu-Wei Huang / Nikoloz Shkriabai / Lorenzo Briganti / Reed Haney / Vineet N KewalRamani / Gregory A Voth / Alan N Engelman / Gregory B Melikyan / Patrick R Griffin / Francisco Asturias / Mamuka Kvaratskhelia / ![]() Abstract: Cellular proteins CPSF6, NUP153 and SEC24C play crucial roles in HIV-1 infection. While weak interactions of short phenylalanine-glycine (FG) containing peptides with isolated capsid hexamers have ...Cellular proteins CPSF6, NUP153 and SEC24C play crucial roles in HIV-1 infection. While weak interactions of short phenylalanine-glycine (FG) containing peptides with isolated capsid hexamers have been characterized, how these cellular factors functionally engage with biologically relevant mature HIV-1 capsid lattices is unknown. Here we show that prion-like low complexity regions (LCRs) enable avid CPSF6, NUP153 and SEC24C binding to capsid lattices. Structural studies revealed that multivalent CPSF6 assembly is mediated by LCR-LCR interactions, which are templated by binding of CPSF6 FG peptides to a subset of hydrophobic capsid pockets positioned along adjoining hexamers. In infected cells, avid CPSF6 LCR-mediated binding to HIV-1 cores is essential for functional virus-host interactions. The investigational drug lenacapavir accesses unoccupied hydrophobic pockets in the complex to potently impair HIV-1 inside the nucleus without displacing the tightly bound cellular cofactor from virus cores. These results establish previously undescribed mechanisms of virus-host interactions and antiviral action. | ||||||
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-Validation report
Summary document | ![]() | 2.2 MB | Display | ![]() |
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Full document | ![]() | 2.2 MB | Display | |
Data in XML | ![]() | 88.3 KB | Display | |
Data in CIF | ![]() | 121.7 KB | Display | |
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-Related structure data
Related structure data | ![]() 4u0bS S: Starting model for refinement C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Assembly
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