1KYC

CRYSTAL STRUCTURE OF A DE NOVO DESIGNED TRIMERIC COILED-COIL PEPTIDE STABLIZED BY IONIC INTERACTIONS

Summary for 1KYC

• Entry DOI: 10.2210/pdb1kyc/pdb
• Related: 1HQJ
• Descriptor: SIN-GLU-GLU-LEU-ARG-ARG-ARG-ILE-GLU-GLU-LEU-GLU-ARG-ARG-ILE-ARG-NH2, SULFATE ION, SUCCINIC ACID, ... (4 entities in total)
• Functional Keywords: coiled coil, de novo design, alpha-helix, trimer, de novo protein
• Biological source: synthetic construct
• Total number of polymer chains: 1
• Total formula weight: 2367.60

Authors

Burkhard, P.,Ivaninskii, S.,Lustig, A. (deposition date: 2002-02-04, release date: 2002-08-07, Last modification date: 2023-08-16)

Primary citation

Burkhard, P.,Ivaninskii, S.,Lustig, A.
Improving coiled-coil stability by optimizing ionic interactions.
J.Mol.Biol., 318:901-910, 2002

PubMed Abstract: Alpha-helical coiled coils are a common protein oligomerization motif stabilized mainly by hydrophobic interactions occurring along the coiled-coil interface. We have recently designed and solved the structure of a two-heptad repeat coiled-coil peptide that is stabilized further by a complex network of inter- and intrahelical salt-bridges in addition to the hydrophobic interactions. Here, we extend and improve the de novo design of this two heptad-repeat peptide by four newly designed peptides characterized by different types of ionic interactions. The contribution of these different types of ionic interactions to coiled-coil stability are analyzed by CD spectroscopy and analytical ultracentrifugation. We show that all peptides are highly alpha-helical and two of them are 100% dimeric under physiological conditions. Furthermore, we have solved the X-ray structure of the most stable of these peptides and the rational design principles are verified by comparing this structure to the structure of the parent peptide. We show that by combining the most favorable inter- and intrahelical salt-bridge arrangements it is possible to design coiled-coil oligomerization domains with improved stability properties.

PubMed: 12054832
DOI: 10.1016/S0022-2836(02)00114-6

Experimental method

X-RAY DIFFRACTION (1.45 Å)