South African mutations of the CCR5 coreceptor for HIV modify interaction with chemokines and HIV Envelope protein.

The CCR5 chemokine receptor is the major coreceptor for HIV-1 and the receptor for CC-chemokines, MIP-1alpha, MIP-1beta, and regulated upon activation normal T-cell-expressed and secreted. Individuals, who are homozygous for the nonfunctional CCR5Delta32 allele, are largely resistant to HIV-1 infection. Four unique mutations that affect the amino acid sequence of CCR5 have been identified in South Africa.

High-affinity binding of southern African HIV type 1 subtype C envelope protein, gp120, to the CCR5 coreceptor.

HIV-1 subtype C is the fastest spreading subtype worldwide and predominantly uses the CCR5 coreceptor, showing minimal transition to the X4 phenotype. This raises the possibility that envelope proteins of HIV-1 subtype C have structural features that favor interaction with CCR5. Preference for CCR5 could arise from enhanced affinity of HIV-1 subtype C for CCR5.

Pro7.33(303) of the human GnRH receptor regulates selective binding of mammalian GnRH.

Mammalian gonadotropin releasing hormone (GnRH) receptors have a conserved acidic residue (Glu7.32(301) or Asp7.32(302)) in extracellular loop (ECL) three that confers selectivity for mammalian GnRH, which has Arg8.