1U0I
IAAL-E3/K3 heterodimer
Summary for 1U0I
| Entry DOI | 10.2210/pdb1u0i/pdb |
| NMR Information | BMRB: 6260 |
| Descriptor | IAAL-E3, IAAL-K3 (2 entities in total) |
| Functional Keywords | coiled-coil, de novo protein |
| Total number of polymer chains | 2 |
| Total formula weight | 4571.50 |
| Authors | Lindhout, D.A.,Litowski, J.R.,Mercier, P.,Hodges, R.S.,Sykes, B.D. (deposition date: 2004-07-13, release date: 2004-10-19, Last modification date: 2024-05-22) |
| Primary citation | Lindhout, D.A.,Litowski, J.R.,Mercier, P.,Hodges, R.S.,Sykes, B.D. NMR solution structure of a highly stable de novo heterodimeric coiled-coil Biopolymers, 75:367-375, 2004 Cited by PubMed Abstract: The NMR solution structure of a highly stable coiled-coil IAAL-E3/K3 has been solved. The E3/K3 coiled-coil is a 42-residue de novo designed coiled-coil comprising three heptad repeats per subunit, stabilized by hydrophobic contacts within the core and electrostatic interactions at the interface crossing the hydrophobic core which direct heterodimer formation. This E3/K3 domain has previously been shown to have high alpha-helical content as well as possessing a low dissociation constant (70 nM). The E3/K3 structure is completely alpha-helical and is an archetypical coiled-coil in solution, as determined using a combination of (1)H-NOE and homology based structural restraints. This structure provides a structural framework for visualizing the important interactions for stability and specificity, which are key to protein engineering applications such as affinity purification and de novo design. PubMed: 15457434DOI: 10.1002/bip.20150 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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