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Lehrstuhl für Biotechnik
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  1. Friedrich-Alexander-Universität
  2. Naturwissenschaftliche Fakultät
  3. Department Biologie

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  3. Probing protein architecture / protein design
  4. Design of a chain-specific heterodimeric variant of TetR

Design of a chain-specific heterodimeric variant of TetR

Bereichsnavigation: Research
  • De novo structure determination using X-ray crystallography
    • DasR
    • pUL50-pUL53
  • Probing protein architecture / protein design
    • Design of a chain-specific heterodimeric variant of TetR
  • Publications
  • Downloads

Design of a chain-specific heterodimeric variant of TetR

The specificity and selectivity of protein-protein interactions are of central importance for many biological processes. We used the in-house side-chain packing program MUMBO to computationally design a chain-specific heterodimeric variant of the bacterial transcription regulator tetracycline repressor (TetR), called T-AB. Our goal was to engineer two different TetR chain variants, A and B, that no longer interact as AA or BB homodimers but selectively recombine to form heterodimers. Although 56 residues from each chain contribute to a dimer interface as large as 2200 Å(2) in wild-type TetR, the substitution of only three residues in one chain and two residues in a second chain sufficed for generating specificity in a T-AB heterodimer variant. The design was corroborated in vivo by a cell-based transcription assay, and in vitro by CD spectroscopy and X-ray crystallography.

J Mol Biol. 2010; 403: 371-385 (PMID: 20816982).

Stereodarstellung einer mittels Computer vorhergesagter bevorzugten Seitenkettenpackung.
Stereographic representation of the computationally predicted favorable side-chain packing.
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