Tetrapeptide derived inhibitors of complexation of a class II MHC: the peptide backbone is not inviolate.
Major histocompatabilty (MHC) proteins rely heavily on peptide backbone recognition for ligation. Nonetheless, modifications to the polyamide backbone of a tetrapeptide ligand can be made without abrogating binding.
Jones
A B
AB
Department of Basic Medicinal Chemistry, Merck Research Laboratories, Rahway, NJ 07065, USA.
Acton
J J
JJ
Rivetna
M N
MN
Cummings
R T
RT
Cubbon
R M
RM
Nichols
E A
EA
Schwartz
C D
CD
Wicker
L S
LS
Hermes
J D
JD
D001665:Binding Sites; D015798:HLA-DR1 Antigen / Q000187:drug effects / Q000378:metabolism; D006388:Hemagglutinins / Q000737:chemistry; D000949:Histocompatibility Antigens Class II / Q000187:drug effects* / Q000378:metabolism*; D020128:Inhibitory Concentration 50; D007769:Lactams / Q000737:chemistry; D008024:Ligands; D018716:Molecular Mimicry; D015394:Molecular Structure; D010455:Peptides / Q000737:chemistry* / Q000494:pharmacology*; D010750:Phosphoproteins / Q000187:drug effects / Q000378:metabolism; D013329:Structure-Activity Relationship; D014157:Transcription Factors / Q000187:drug effects / Q000378:metabolism
D015798:HLA-DR1 Antigen; D006388:Hemagglutinins; D000949:Histocompatibility Antigens Class II; D007769:Lactams; D008024:Ligands; D010455:Peptides; D010750:Phosphoproteins; D014157:Transcription Factors; C075995:down-regulator of transcription 1