2MNQ
1H, 13C, and 15N Chemical Shift Assignments for Thymosin alpha 1
Summary for 2MNQ
| Entry DOI | 10.2210/pdb2mnq/pdb |
| NMR Information | BMRB: 19901 |
| Descriptor | THYMOSIN ALPHA-1 (1 entity in total) |
| Functional Keywords | protein binding, hormone peptide, membrane interaction |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: P06454 |
| Total number of polymer chains | 1 |
| Total formula weight | 3096.31 |
| Authors | Nepravishta, R.,Mandaliti, W.,Eliseo, T.,Sinibaldi Vallebona, P.,Pica, F.,Garaci, E.,Paci, M. (deposition date: 2014-04-09, release date: 2015-03-04, Last modification date: 2024-10-16) |
| Primary citation | Nepravishta, R.,Mandaliti, W.,Eliseo, T.,Sinibaldi Vallebona, P.,Pica, F.,Garaci, E.,Paci, M. Thymosin alpha 1 inserts N terminus into model membranes assuming a helical conformation. Expert Opin Biol Ther, 15 Suppl 1:71-81, 2015 Cited by PubMed Abstract: Thymosin α1 (Tα1) is a peptide hormone whose therapeutic application has been approved in several diseases, but the description of a precise receptor for its therapeutic action still remains elusive and some knowledge of the mechanism of interaction with the cell membrane still needs to be clarified. This work is aimed at studying the folding and interaction of Tα1, which is completely unstructured in water solution, with model membranes. PubMed: 25642593DOI: 10.1517/14712598.2015.1009034 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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