3u29 Citations

Structural insights into charge pair interactions in triple helical collagen-like proteins.

J Biol Chem 287 8039-47 (2012)
Related entries: 3t4f, 6vzx

Cited: 36 times
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Abstract

The collagen triple helix is the most abundant protein fold in humans. Despite its deceptively simple structure, very little is understood about its folding and fibrillization energy landscape. In this work, using a combination of x-ray crystallography and nuclear magnetic resonance spectroscopy, we carry out a detailed study of stabilizing pair-wise interactions between the positively charged lysine and the negatively charged amino acids aspartate and glutamate. We find important differences in the side chain conformation of amino acids in the crystalline and solution state. Structures from x-ray crystallography may have similarities to the densely packed triple helices of collagen fibers whereas solution NMR structures reveal the simpler interactions of isolated triple helices. In solution, two distinct types of contacts are observed: axial and lateral. Such register-specific interactions are crucial for the understanding of the registration process of collagens and the overall stability of proteins in this family. However, in the crystalline state, there is a significant rearrangement of the side chain conformation allowing for packing interactions between adjacent helices, which suggests that charged amino acids may play a dual role in collagen stabilization and folding, first at the level of triple helical assembly and second during fibril formation.

Articles - 3u29 mentioned but not cited (3)

  1. Structural insights into charge pair interactions in triple helical collagen-like proteins. Fallas JA, Dong J, Tao YJ, Hartgerink JD. J Biol Chem 287 8039-8047 (2012)
  2. Peptide tessellation yields micrometre-scale collagen triple helices. Tanrikulu IC, Forticaux A, Jin S, Raines RT. Nat Chem 8 1008-1014 (2016)
  3. The role of cross-chain ionic interactions for the stability of collagen model peptides. Keshwani N, Banerjee S, Brodsky B, Makhatadze GI. Biophys J 105 1681-1688 (2013)


Reviews citing this publication (5)

  1. Nanomaterials design and tests for neural tissue engineering. Saracino GA, Cigognini D, Silva D, Caprini A, Gelain F. Chem Soc Rev 42 225-262 (2013)
  2. Self-assemble peptide biomaterials and their biomedical applications. Chen J, Zou X. Bioact Mater 4 120-131 (2019)
  3. Rational design of fiber forming supramolecular structures. Kumar VA, Wang BK, Kanahara SM. Exp Biol Med (Maywood) 241 899-908 (2016)
  4. Pairwise interactions in collagen and the design of heterotrimeric helices. Jalan AA, Hartgerink JD. Curr Opin Chem Biol 17 960-967 (2013)
  5. Glycoproteins functionalized natural and synthetic polymers for prospective biomedical applications: A review. Tabasum S, Noreen A, Kanwal A, Zuber M, Anjum MN, Zia KM. Int J Biol Macromol 98 748-776 (2017)

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