Protein interactions
Protein |
Gene |
Interaction |
Pubs |
Envelope surface glycoprotein gp160, precursor
|
env
|
The calmodulin-binding domains in HIV-1 gp160 are involved in Fas-mediated apoptosis |
PubMed
|
|
env
|
The carboxyl-terminal domains (residues 768-788 and 826-854) of HIV-1 gp160 bind to calmodulin (CaM) |
PubMed
|
Envelope transmembrane glycoprotein gp41
|
env
|
The carboxyl terminus (amino acid residues 768-788 and 828-855) of HIV-1 gp41 binds efficiently to purified calmodulin (CaM) and inhibits in vitro CaM-mediated stimulation of phosphodiesterase activity |
PubMed
|
|
env
|
The fusion between CD4+ human cells and cells stably expressing HIV-1 gp41 and gp120 is inhibited by calmodulin |
PubMed
|
Nef
|
nef
|
HIV-1 Nef induces interleukin 10 expression through an interaction with the calcium/calmodulin-dependent phosphodiesterase signal transduction pathway |
PubMed
|
|
nef
|
HIV-1 Nef-induced CCL-2/MCP-1 upregulation in astrocytes depends on the myristoylation moiety (residues 2-3) of Nef and requires functional calmodulin |
PubMed
|
|
nef
|
Fluorescence spectroscopy analyses indicate the myristoylated N-terminal eight amino acids of HIV-1 Nef directly interact with calcium bound calmodulin |
PubMed
|
matrix
|
gag
|
An HIV-1 MA peptide (residues 8-43) binds to CaM with a very high affinity with dissociation constant 25 nm |
PubMed
|
|
gag
|
Calmodulin (CaM) binding to HIV-1 MA induces the extrusion of the myristate group, suggesting that hydrophobic contacts between CaM and MA are critical for binding |
PubMed
|
|
gag
|
Calmodulin binds to both HIV-1 Gag and Matrix proteins through an extended calmodulin-binding domain in Matrix (amino acids 11-46) |
PubMed
|
Go to the HIV-1, Human Interaction Database