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Sequence similarity between opioid peptide precursors and DNA‐binding proteins
Author(s) -
Bakalkin Georgy Ya.,
Ponomariev Dmitry,
Sarkisyan Raphik A.,
Terenius Lars
Publication year - 1991
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(91)80471-e
Subject(s) - opioid peptide , peptide , zinc finger , enkephalin , dna , biology , helix (gastropod) , basic helix loop helix , chemistry , dna binding protein , biochemistry , transcription factor , biophysics , gene , opioid , receptor , snail , ecology
The opioid peptide precursors, preprodynorphin and preproenkephalin show structure similarity with a transcription factor, hunchback and the putative helix‐loop‐helix DNA‐binding proteins, lil‐1 , tal and twist . Segments with similarity contain the three enkephalin sequences in preprodynorphin and one in preproenkephalin which are present within heptapeptide repeats characteristic of an α‐helical coiled‐coil structure distinctive of an amphipathic helix‐loop‐helix DNA‐binding motif, Hunchback and the opioid prohormones also have cystein‐rich regions characteristic of zinc‐finger domains in common.