Collagen Stabilization at Atomic Level

• DOI: 10.1016/s0969-2126(03)00025-x
• Publication Date: 2003-03-15T10:04:18Z
• Authors: Jörg Stetefeld; Sabine Frank; Margrit Jenny; Therese Schulthess; Richard A. Kammerer; Sergei Boudko; Ruth Landwehr; Kenji Okuyama; Jürgen Engel
• Keywords: 0303 health sciences; collagen stability; Polymers; Crystallography, X-Ray; Protein Engineering; Protein Structure, Tertiary; NC domain; 03 medical and health sciences; Structural Biology; hetero assembly; Animals; Humans; Collagen; protein design; Peptides; foldon; Molecular Biology; collagen folding

In a designed fusion protein the trimeric domain foldon from bacteriophage T4 fibritin was connected to the C terminus of the collagen model peptide (GlyProPro)(10) by a short Gly-Ser linker to facilitate formation of the three-stranded collagen triple helix. Crystal structure analysis at 2.6 A resolution revealed conformational changes within the interface of both domains compared with the structure of the isolated molecules. A striking feature is an angle of 62.5 degrees between the symmetry axis of the foldon trimer and the axis of the triple helix. The melting temperature of (GlyProPro)(10) in the designed fusion protein (GlyProPro)(10)foldon is higher than that of isolated (GlyProPro)(10,) which suggests an entropic stabilization compensating for the destabilization at the interface.