Selected article for: "class iii vfp and fusion loop"
Author: Melnik, Lilia I; Garry, Robert F; Morris, Cindy A
Title: Peptide inhibition of human cytomegalovirus infection
  • Document date: 2011_2_22
    • ID: 0p6x4lwx_10
    Snippet: The Wimley-White Interfacial Hydrophobicity Scale (WWIHS) is an experimentally determined hydrophobicity scale that provides a quantitative description of a protein partitioning and folding into membrane interfaces. WWIHS score-positive sequences may also interact with hydrophobic surfaces within proteins, and are often sequestered within pre-fusion forms of viral fusion proteins. In addition to similarities in the overall structure of the post-f.....
    Document: The Wimley-White Interfacial Hydrophobicity Scale (WWIHS) is an experimentally determined hydrophobicity scale that provides a quantitative description of a protein partitioning and folding into membrane interfaces. WWIHS score-positive sequences may also interact with hydrophobic surfaces within proteins, and are often sequestered within pre-fusion forms of viral fusion proteins. In addition to similarities in the overall structure of the post-fusion forms of class III VFP, there are additional similarities in the distribution of WWIHSpositive sequences (Figure 1 , red). The similarities include at least one extended "fusion loop" in the fusion domain (domain II), and one or more WWIHS scorepositive sequences in domain III. With the exception of the ACNPV GP64, each of these proteins contains another WWIHS positive domain II sequence near the "hinge" region adjacent to the domain. Herpesvirus gB proteins have an additional WWIHS scale score-positive sequence in domain I. In the case of class II and III viral fusion proteins, the fusion loops in the fusion domain often contain sequences with positive WWIHS scores.

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