Premium
‘Molecular sandwiches’ as a basis for structural and functional similarities of interferons, MSH, ACTH, LHRH, myelin basic protein, and albumins
Author(s) -
Root-Bernstein Robert Scott
Publication year - 1984
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(84)80247-1
Subject(s) - ovalbumin , myelin basic protein , peptide , chemistry , hormone , muramyl dipeptide , tetrapeptide , biochemistry , medicine , tryptophan , dipeptide , endocrinology , human serum albumin , myelin , biology , immunology , amino acid , immune system , central nervous system , in vitro
Sequential similarities between the tryptohan peptide of myelin basic protein (residues 111–121), luteinizing hormone releasing hormone, melanotropin, adrenocorticotropin (residues 1–13), human leukocyte interferon (residues 28–40), and various segments of human and bovine serum albumin and hen ovalbumin are presented. It is suggested that these structural similarities may explain observations concerning common functional characteristics such as serotonin modulation, immunological activity with the adjuvant muramyl dipeptide, immunological cross‐reactivity, and the possible MSH‐ACTH‐like activity of a pepsin‐derived peptide of interferon.