Structural and Functional Characterization of a Constrained Asx-Turn Motif
Abstract
The specific and timely glycosylation of proteins is associated with the proper structure, function, and targeting of glycoprotein conjugates. For N-linked glycosylation, catalyzed by the enzyme oligosaccharyl transferase (OT), we have recently proposed that the fidelity of this modification may be associated with particular conformational tendencies of polypeptide substrates which contain the consensus sequence Asn-Xaa-Thr/Ser. The presence of a local Asx-turn ,about the Asn-Xaa-Thr/Ser sequence, is central to this proposal, which was based on studies of the glycosyl acceptor properties of linear and cyclic peptides. Herein, we describe a new substrate for N-linked glycosylation which is conformationally constrained to adopt an Asx-turn and specifically designed to test this proposal.
Additional Information
© 1994 American Chemical Society. Received June 7, 1994. This research was supported by National Institutes of Health Grant GM39334 and an NSF predoctoral fellowship to M.D.S. B.I. also gratefully acknowledges support from the Alfred P. Sloan Foundation, the Camille and Henry Dreyfus Teacher-Scholar Program, and Zeneca Inc. We acknowledge the Dorothy Chandler, Camilla Chandler Frost Laboratory in Biology at Caltech for use of NMR instrumentation (Varian Unity Plus 600 Spectrometer).Attached Files
Supplemental Material - ja00097a083_si_001.pdf
Supplemental Material - ja8424.pdf
Files
| Name | Size | Download all |
|---|---|---|
|
md5:5f057d91468ab52a6744e8cda42410fb
|
2.3 MB | Preview Download |
|
md5:fda7fe4adb53757729d7476cf180c9a9
|
747.4 kB | Preview Download |
Additional details
- Eprint ID
- 86767
- DOI
- 10.1021/ja00097a083
- Resolver ID
- CaltechAUTHORS:20180601-162823795
- GM39334
- NIH
- NSF Predoctoral Fellowship
- Alfred P. Sloan Foundation
- Camille and Henry Dreyfus Foundation
- Zeneca
- Created
-
2018-06-04Created from EPrint's datestamp field
- Updated
-
2021-11-15Created from EPrint's last_modified field