1u0i
From Proteopedia
IAAL-E3/K3 heterodimer
Overview
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.
About this Structure
Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sat May 3 10:36:00 2008
