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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
Author(s) -
Samuel Kenneth P.,
Seth Arun,
Konopka Andrzej,
Lautenberger James A.,
Papas Takis S.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81023-2
Subject(s) - biology , protein kinase a , phosphorylation , microbiology and biotechnology , protein kinase r , protein kinase domain , mitogen activated protein kinase kinase , biochemistry , gene , mutant
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).