The 3′‐orf protein of human immunodeficiency virus shows structural homology with the phosphorylation domain of human interleukin‐2 receptor and the ATP‐binding site of the protein kinase family

[摘要]

The primary amino acid sequence within a stretch of 25 residues (positions 91–116) of the middle portion of the 3-′orf protein (p27^3′-orf) of the human immunodeficiency virus (HIV) shares structural homology with a highly charged region within the intracytoplasmic phosphorylation domain of human interleukin-2 receptor (IL-2R) and the ATP-binding site of the catalytic subunit of cAMP-dependent protein kinase (cAMP-PK) and other members of the protein kinase family. Comparison of the predicted secondary structure within this region of p27^3′-orf with the phosphorylation domain of human IL-2R and the ATP-binding region of the phospho-kinase family of protein suggests that the 3′-orf protein could serve homologous function(s).

[学科分类] 生物化学/生物物理

[关键词] 3′-orf protein;IL-2 receptor;Phosphorylation domain;ATP-binding site;Protein kinase family;Human immunodeficiency virus;HIV;human immunodeficiency virus;IL-2R;interleukin-2 receptor;orf;open reading frame;AIDS;acquired immune deficiency syndrome;ARC;AIDS-related complex;cAMP-PK;cyclic AMP-dependent protein kinase;cGMP-PK;cyclic GMP-dependent protein kinase;phos.b-K;γ-subunit of rabbit skeletal muscle phosphorylase b kinase;Xaa;any amino acid