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Figure 1 | Virology Journal

Figure 1

From: The role of myristoylation in the membrane association of the Lassa virus matrix protein Z

Figure 1

Schematic representation of LASV Z protein. Amino acids associated with particular structures and functions are shown in single letters. The myristoylated glycine residue at amino acid position 2 is shown in bold letters. Cysteine- and histidine residues forming the RING finger domain (C, cysteine; H, histidine) as well as the late domain motifs PPPY and PTAP (P, proline; Y, tyrosine; T, threonine; A, alanine) are indicated. Alignment of the N-termini of Old and New World arenavirus Z protein sequences are shown. Conserved glycine residues at position 2 are highlighted in bold letters. To generate the non-myristoylated mutant Z-G2A of LASV Z protein, site-directed mutagenesis was used to change the N-terminal glycine codon to an alanine codon.

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