2JTA

NMR structure of immunosuppressory ubiquitin fragment is similar to related ubiquitin region.

Summary for 2JTA

Entry DOI	10.2210/pdb2jta/pdb
Descriptor	10-mer ubiquitin peptide (1 entity in total)
Functional Keywords	alpha helix, immunosuppression, ubiquitin, signaling protein
Total number of polymer chains	1
Total formula weight	1169.22
Authors	Jaremko, M.,Jaremko, L.,Zhukov, I.,Cebrat, M. (deposition date: 2007-07-21, release date: 2008-07-29, Last modification date: 2024-05-29)
Primary citation	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, 91:423-431, 2009 Cited by PubMed Abstract: 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. PubMed: 19213045 DOI: 10.1002/bip.21160 PDB entries with the same primary citation
Experimental method	SOLUTION NMR

Structure validation