2L9I
NMR structure of thymosin alpha-1
Summary for 2L9I
| Entry DOI | 10.2210/pdb2l9i/pdb |
| NMR Information | BMRB: 17458 |
| Descriptor | Thymosin alpha-1 (1 entity in total) |
| Functional Keywords | lymphocyte membrane binding peptide, t-cell differentiation, immunopotentiation, transcription, peptide binding protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: P06454 |
| Total number of polymer chains | 1 |
| Total formula weight | 3096.31 |
| Authors | Elizondo-Riojas, M.A.,Gorenstein, D.G.,Volk, D.E. (deposition date: 2011-02-11, release date: 2011-12-28, Last modification date: 2024-11-27) |
| Primary citation | Elizondo-Riojas, M.A.,Chamow, S.M.,Tuthill, C.W.,Gorenstein, D.G.,Volk, D.E. NMR structure of human thymosin alpha-1. Biochem.Biophys.Res.Commun., 416:356-361, 2011 Cited by PubMed Abstract: 800 MHz NMR structure of the 28-residue peptide thymosin alpha-1 in 40% TFE/60% water (v/v) has been determined. Restrained molecular dynamic simulations with an explicit solvent box containing 40% TFE/60% TIP3P water (v/v) were used, in order to get the 3D model of the NMR structure. We found that the peptide adopts a structured conformation having two stable regions: an alpha-helix region from residues 14 to 26 and two double β-turns in the N-terminal twelve residues which form a distorted helical structure. PubMed: 22115779DOI: 10.1016/j.bbrc.2011.11.041 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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