A turn-like structure "KKPE" segment mediates the specific binding of viral protein A27 to heparin and heparan sulfate on cell surfaces.

@article{Shih2009ATS,
  title={A turn-like structure "KKPE" segment mediates the specific binding of viral protein A27 to heparin and heparan sulfate on cell surfaces.},
  author={Ping-Chen Shih and Min-Shiang Yang and S Lin and Yu Ho and J S Hsiao and Da-Rong Wang and Steve S-F Yu and W Chang and Der-Lii M. Tzou},
  journal={The Journal of biological chemistry},
  year={2009},
  volume={284 52},
  pages={36535-46}
}
Vaccinia viral envelope protein A27 (110 amino acids) specifically interacts with heparin (HP) or heparan sulfate (HS) proteoglycans for cell surface attachment. To examine the binding mechanism, a truncated soluble form of A27 (sA27-aa; residues 21-84 of A27) with Cys(71) and Cys(72) mutated to Ala was used as the parent molecule. sA27-aa consists of two structurally distinct domains, a flexible Arg/Lys-rich heparin-binding site (HBS) (residues 21-32; (21)STKAAKKPEAKR(32)) and a rigid coiled… CONTINUE READING

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