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Publication Abstract from PubMed

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.

NMR solution structure of a highly stable de novo heterodimeric coiled-coil.,Lindhout DA, Litowski JR, Mercier P, Hodges RS, Sykes BD Biopolymers. 2004 Dec 5;75(5):367-75. PMID:15457434^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.