Peptide-binding specificity of the molecular chaperone BiP Journal Article
| Authors: | Flynn, G. C.; Pohl, J.; Flocco, M. T.; Rothman, J. E. |
| Article Title: | Peptide-binding specificity of the molecular chaperone BiP |
| Abstract: | Members of the heat-shock protein family (hsp70s) can distinguish folded from unfolded proteins. This property is crucial to the role of hsp70s as molecular chaperones and is attributable to the amino-acid specificity of the peptide-binding site. The specificity for peptide ligands is investigated using a set of peptides of random sequence but defined chain length. The peptide-binding site selects for aliphatic residues and accommodates them in an environment energetically equivalent to the interior of a folded protein. © 1991 Nature Publishing Group. |
| Keywords: | protein conformation; amino acid sequence; molecular sequence data; peptides; thermodynamics; binding sites; amino acids; protein folding; ligand binding; fungal proteins; binding, competitive; heat-shock proteins; heat shock protein; priority journal; article; support, non-u.s. gov't; support, u.s. gov't, p.h.s.; adenosinetriphosphatase; chemistry, physical; chaperonin |
| Journal Title: | Nature |
| Volume: | 353 |
| Issue: | 6346 |
| ISSN: | 0028-0836 |
| Publisher: | Nature Publishing Group |
| Date Published: | 1991-10-24 |
| Start Page: | 726 |
| End Page: | 730 |
| Language: | English |
| DOI: | 10.1038/353726a0 |
| PUBMED: | 1834945 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Source: Scopus |
