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NMR solution structure of a highly stable de novo heterodimeric coiled‐coil
Author(s) -
Lindhout Darrin A.,
Litowski Jennifer R.,
Mercier Pascal,
Hodges Robert S.,
Sykes Brian D.
Publication year - 2004
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20150
Subject(s) - coiled coil , chemistry , protein design , crystallography , protein subunit , dissociation constant , protein engineering , structural motif , protein structure , stereochemistry , biochemistry , receptor , gene , enzyme
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 α‐helical content as well as possessing a low dissociation constant (70 nM). The E3/K3 structure is completely α‐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. © 2004 Wiley Periodicals, Inc. Biopolymers, 2004