Structure-function analysis of human interleukin-6. Evidence for the involvement of the carboxy-terminus in function.
C-terminally deleted analogs of human interleukin-6 (IL-6) have been constructed at the cDNA level, and after cell-free transcription and translation their biological activity was analyzed. Removal of only 4 amino acids resulted in complete loss of biological activity as determined by the B9 cell proliferation assay. Secondary structure prediction of human IL-6 resulted in 58% helix, 14% beta-structure, and 28% turn and coil (average of 3 independent methods). The circular dichroism of recombinant human IL-6 was measured in the near and far UV. Evaluation of the latter in terms of secondary structures gave 67% helix, 15% beta-structure, and 18% turn and coil.
Krüttgen
A
A
Institut für Biochemie der RWTH Aachen, FRG.
Rose-John
S
S
Möller
C
C
Wroblowski
B
B
Wollmer
A
A
Müllberg
J
J
Hirano
T
T
Kishimoto
T
T
Heinrich
P C
PC
D000818:Animals; D002460:Cell Line; D002942:Circular Dichroism; D004247:DNA / Q000032:analysis; D006801:Humans; D015850:Interleukin-6 / Q000235:genetics; D009154:Mutation; D014176:Protein Biosynthesis; D011487:Protein Conformation; D051381:Rats; D013329:Structure-Activity Relationship; D014158:Transcription, Genetic
D015850:Interleukin-6; D004247:DNA