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Tetrapeptide derived inhibitors of complexation of a class II MHC: the peptide backbone is not inviolate.

Jones AB., Acton JJ., Rivetna MN., Cummings RT., Cubbon RM., Nichols EA., Schwartz CD., Wicker LS., Hermes JD.

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.

More information Original publication

DOI

10.1016/s0960-894x(99)00333-9

Type

Journal article

Publication Date

1999-07-01T00:00:00+00:00

Volume

9

Pages

2109 - 2114

Total pages

5

Addresses

D, e, p, a, r, t, m, e, n, t, , o, f, , B, a, s, i, c, , M, e, d, i, c, i, n, a, l, , C, h, e, m, i, s, t, r, y, ,, , M, e, r, c, k, , R, e, s, e, a, r, c, h, , L, a, b, o, r, a, t, o, r, i, e, s, ,, , R, a, h, w, a, y, ,, , N, J, , 0, 7, 0, 6, 5, ,, , U, S, A, .

Keywords

Lactams, Peptides, Phosphoproteins, Transcription Factors, Hemagglutinins, Histocompatibility Antigens Class II, HLA-DR1 Antigen, Ligands, Inhibitory Concentration 50, Binding Sites, Molecular Mimicry, Molecular Structure, Structure-Activity Relationship