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- W1978014671 abstract "We have used affinity panning of libraries of bacteriophages that display random octapeptide or dodecapeptide sequences at the N-terminus of the adsorption protein (pIII) to characterize peptides that bind to the endoplasmic reticulum chaperone BiP and to develop a scoring system that predicts potential BiP-binding sequences in naturally occurring polypeptides. BiP preferentially binds peptides containing a subset of aromatic and hydrophobic amino acids in alternating positions, suggesting that peptides bind in an extended conformation, with the side chains of alternating residues pointing into a cleft on the BiP molecule. Synthetic peptides with sequences corresponding to those displayed by BiP-binding bacteriophages bind to BiP and stimulate its ATPase activity, with a half-maximal concentration in the range 10-60 microM." @default.
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- W1978014671 date "1993-11-19" @default.
- W1978014671 modified "2023-10-14" @default.
- W1978014671 title "Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP" @default.
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- W1978014671 doi "https://doi.org/10.1016/0092-8674(93)90492-9" @default.
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