Title: Primary sequence domains required for the retention of rotavirus VP7 in the endoplasmic reticulum Document date: 1988_11_1
ID: 63mxzwti_4
Snippet: Amino acids of VP7 are depicted by letter code and the various restriction sites used for constructing the VP7 mutants lacking the first initiation codon and hydrophobic domain (dhl series) or the VP7 amylase-chimeric molecules are shown (Fig. 1, A and B) . The VP7 genes used in this study differed from the previously published VP7 sequence (5) at three positions, Cys32 to Phe, Leu~ to Phe and Thr65 to lie, and were confirmed by dideoxy sequencin.....
Document: Amino acids of VP7 are depicted by letter code and the various restriction sites used for constructing the VP7 mutants lacking the first initiation codon and hydrophobic domain (dhl series) or the VP7 amylase-chimeric molecules are shown (Fig. 1, A and B) . The VP7 genes used in this study differed from the previously published VP7 sequence (5) at three positions, Cys32 to Phe, Leu~ to Phe and Thr65 to lie, and were confirmed by dideoxy sequencing (34) of our chimeric clones (see below). VP7 mutants deleted in the region immediately proximal to residue 62 had Ser62 changed to Ala as previously shown (31) .
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