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| DIFFERENT CONFORMATIONS FOR THE SAME POLYPEPTIDE BOUND TO CHAPERONES DNAK AND GROEL |
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| Author(s): LANDRY SJ, JORDAN R, MCMACKEN R, GIERASCH LM |
| Source: NATURE Volume: 355 Issue: 6359 Pages: 455-457 Published: JAN 30 1992 |
| Times Cited: 270 References: 13 |
| Abstract: THE proteins DnaK (hsp70) and GroEL (cpn60) from Escherichia coli are prototypes of two classes of molecular chaperones conserved throughout evolution 1. The analysis of transferred nuclear Overhauser effects in two-dimensional NMR spectra is ideally suited to determine chaperone-bound conformations of peptides 2. The peptide vsv-C (amino-acid sequence KLIGVLSSLFRPK) stimulates the ATPase of BiP and Hsc70 (ref. 3) and the intrinsic ATPase of DnaK. The affinity of the vsv-C peptide for DnaK is greatly reduced in the presence of ATP. Here we analyse transferred nuclear Overhauser effects and show that the peptide is in an extended conformation while bound to DnaK but is helical when bound to GroEL. NMR also indicates that the mobility of the peptide backbone is reduced more by binding to DnaK than by binding to GroEL, whereas the side chains are less mobile when bound to GroEL. |
| Document Type: Article |
| Language: English |
| Reprint Address: LANDRY, SJ (reprint author), UNIV TEXAS, SW MED CTR, DEPT PHARMACOL, 5323 HARRY HINES BLVD, DALLAS, TX 75235 USA |
Addresses:
1. JOHNS HOPKINS UNIV, SCH HYG & PUBL HLTH, DEPT BIOCHEM, BALTIMORE, MD 21205 USA |
| Publisher: MACMILLAN MAGAZINES LTD, PORTERS SOUTH, 4 CRINAN ST, LONDON, ENGLAND N1 9XW |
| Subject Category: Multidisciplinary Sciences |
| IDS Number: HB530 |
| ISSN: 0028-0836 |
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