2TGF
THE SOLUTION STRUCTURE OF HUMAN TRANSFORMING GROWTH FACTOR ALPHA
Summary for 2TGF
| Entry DOI | 10.2210/pdb2tgf/pdb |
| Descriptor | TRANSFORMING GROWTH FACTOR-ALPHA (1 entity in total) |
| Functional Keywords | growth factor |
| Biological source | Homo sapiens (human) |
| Cellular location | Transforming growth factor alpha: Secreted, extracellular space. Protransforming growth factor alpha: Cell membrane; Single-pass type I membrane protein: P01135 |
| Total number of polymer chains | 1 |
| Total formula weight | 5560.25 |
| Authors | Harvey, T.S.,Wilkinson, A.J.,Tappin, M.J.,Cooke, R.M.,Campbell, I.D. (deposition date: 1991-01-23, release date: 1993-04-15, Last modification date: 2024-10-23) |
| Primary citation | Harvey, T.S.,Wilkinson, A.J.,Tappin, M.J.,Cooke, R.M.,Campbell, I.D. The solution structure of human transforming growth factor alpha. Eur.J.Biochem., 198:555-562, 1991 Cited by PubMed Abstract: The solution structure of transforming growth factor alpha has been determined by a combination of high-resolution 1H-nuclear magnetic resonance and distance geometry and restrained molecular dynamics. The 382 restraints derived from the NMR experiments were used to calculate many distance geometry structures, which were then refined by restrained molecular mechanics. Five of these structures were further refined using a variety of methods. Comparison of independently measured parameters, such as calculated hydrogen bonding patterns and experimental amide exchange rates, have been used to evaluate the accuracy of the structures. Also, possible mechanisms to explain the pH-dependent conformational interconversion observed are suggested. Finally comparisons between this work and others on this topic have been made. PubMed: 2050136DOI: 10.1111/j.1432-1033.1991.tb16050.x PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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