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De novo tubular nanostructure design based on self-assembly of beta-helical protein motifs

  1. Author:
    Haspel, N.
    Zanuy, D.
    Aleman, C.
    Wolfson, H.
    Nussinov, R.

  2. Author Address

    NCI, Frederick Canc Res & Dev Ctr, Basic Res Program, SAIC Frederick Inc,Ctr Canc Res Nanobiol Program, Frederick, MD 21702 USA. Tel Aviv Univ, Fac Exact Sci, Sch Comp Sci, IL-69978 Tel Aviv, Israel. UPC, ETSEIB, Dept Chem Engn, E-08028 Barcelona, Spain. Tel Aviv Univ, Sackler Fac Med, Dept Human Genet, Sackler Inst Mol Med, IL-69978 Tel Aviv, Israel.;Nussinov, R, NCI, Frederick Canc Res & Dev Ctr, Basic Res Program, SAIC Frederick Inc,Ctr Canc Res Nanobiol Program, Frederick, MD 21702 USA.;ruthn@ncifcrf.gov
    1. Year: 2006
    2. Date: Jul
  2. Journal: Structure
    1. 14
    2. 7
    3. Pages: 1137-1148
  4. Type of Article: Article
  5. ISSN: 0969-2126
  1. Abstract:

    We present an approach for designing self-assembled ramostructures from naturally occurring building block segments obtained from native protein structures. We focus on structural motifs from left-handed beta-helical proteins. We selected 17 motifs. Copies of each of the motifs are stacked one atop the other. The obtained structures were simulated for long periods by using Molecular Dynamics to test their ability to retain their organization over time. We observed that a structural model based on the self-assembly of a motif from E. coli galactoside acetyltransferase produced a very stable tube. We studied the interactions that help maintain the conformational stability of the systems, focusing on the role of specific amino acids at specific positions. Analysis of these systems and a mutational study of selected candidates revealed that the presence of proline and glycine residues in the loops of P-helical structures greatly enhances the structural stability of the systems.

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External Sources

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  2. DOI: 10.1016/j.str.2006.05.016
  3. View record in Web of Science®
  4. WOS: 000239228500008

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