Structural highlights
Publication Abstract from PubMed
Recently, ubiquitin was suggested as a promising anti-inflammatory protein therapeutic. We found that a peptide fragment corresponding to the ubiquitin(50-59) sequence (LEDGRTLSDY) possessed the immunosuppressive activity comparable with that of ubiquitin. CD and NMR spectroscopies were used to determine the conformational preferences of LEDGRTLSDY in solution. The peptide mixture, obtained by pepsin digestion of ubiquitin, was even more potent than the intact protein. Although the peptide exhibited a well-defined conformation in methanol, its structure was distinct from the corresponding 50-59 fragment in the native ubiquitin molecule. (c) 2009 Wiley Periodicals, Inc. Biopolymers 91: 423-431, 2009.This article was originally published online as an accepted preprint. The "Published Online" date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com.
The immunosuppressive activity and solution structures of ubiquitin fragments.,Jaremko L, Jaremko M, Pasikowski P, Cebrat M, Stefanowicz P, Lisowski M, Artym J, Zimecki M, Zhukov I, Szewczuk Z Biopolymers. 2009 Jun;91(6):423-31. PMID:19213045[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jaremko L, Jaremko M, Pasikowski P, Cebrat M, Stefanowicz P, Lisowski M, Artym J, Zimecki M, Zhukov I, Szewczuk Z. The immunosuppressive activity and solution structures of ubiquitin fragments. Biopolymers. 2009 Jun;91(6):423-31. PMID:19213045 doi:10.1002/bip.21160
