Document Type
Article
Publication Title
Cell
Publication Date
11-19-1993
Volume
75
Issue
4
Disciplines
Biology | Life Sciences
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 (plll) 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 μM.
DOI
https://doi.org/10.1016/0092-8674(93)90492-9
Rights
© 1993 Cell Press
Recommended Citation
Blond-Elguindi, Sylvie; Cwirla, Steven E.; Dower, William J.; Lipshutz, Robert J.; Sprang, Stephen R.; Sambrook, Joseph F.; and Gething, Mary Jane H., "Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP" (1993). Biological Sciences Faculty Publications. 550.
https://scholarworks.umt.edu/biosci_pubs/550