5K86

Aza-glycine containing collagen peptide

Summary for 5K86

• Entry DOI: 10.2210/pdb5k86/pdb
• Descriptor: Aza-glycine containing collagen peptide, SULFATE ION (3 entities in total)
• Functional Keywords: aza-glycine, collagen, triple-helix, structural protein
• Biological source: synthetic construct
• Total number of polymer chains: 3
• Total formula weight: 6694.09

Authors

Chenoweth, D.M.,Kasznel, A.J.,Hai, Y. (deposition date: 2016-05-27, release date: 2017-06-28, Last modification date: 2023-11-15)

Primary citation

Kasznel, A.J.,Zhang, Y.,Hai, Y.,Chenoweth, D.M.
Structural Basis for Aza-Glycine Stabilization of Collagen.
J. Am. Chem. Soc., 139:9427-9430, 2017

PubMed Abstract: Previously, we have demonstrated that replacement of the strictly conserved glycine in collagen with aza-glycine provides a general solution for stabilizing triple helical collagen peptides (Chenoweth, D. M.; et al. J. Am. Chem. Soc. 2016, 138, 9751 ; 2015, 137, 12422 ). The additional hydrogen bond and conformational constraints provided by aza-glycine increases the thermal stability and rate of folding in collagen peptides composed of Pro-Hyp-Gly triplet repeats, allowing for truncation to the smallest self-assembling peptide systems observed to date. Here we show that aza-glycine substitution enhances the stability of an arginine-containing collagen peptide and provide a structural basis for this stabilization with an atomic resolution crystal structure. These results demonstrate that a single nitrogen atom substitution for a glycine alpha-carbon increases the peptide's triple helix melting temperature by 8.6 °C. Furthermore, we provide the first structural basis for stabilization of triple helical collagen peptides containing aza-glycine and we demonstrate that minimal alteration to the peptide backbone conformation occurs with aza-glycine incorporation.

PubMed: 28650147
DOI: 10.1021/jacs.7b03398

Experimental method

X-RAY DIFFRACTION (1.127 Å)