Linked Life Data

2998038

Source:http://linkedlifedata.com/resource/pubmed/id/2998038

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1985-12-12
pubmed:databankReference
pubmed:abstractText
The primary structure of the trypsin cleavage site in the outer layer protein VP3 of rotavirus SA11 was determined. This cleavage enhances the infectivity of rotavirus SA11. Both VP8, one of the polypeptides generated by the cleavage, and VP3 had their alpha-NH2 blocked. Only VP5, the other polypeptide produced by the cleavage, was susceptible to sequential Edman degradation, indicating that it contained the new alpha-NH2 terminus generated by trypsin hydrolysis. The results indicated that purified VP5 is composed of two polypeptides with the following amino acid sequence at their N terminus: (a) ??VYTRAQPNQDAVVSKTS...; (b) AQPNQDAVVSKTS.... Sequencing of the DNA complementary to ds RNA segment 4 revealed a nucleotide sequence encoding the amino acid sequences indicated above, with only one different amino acid. From these results, the amino acid sequence of the site cleaved by trypsin was extended to cover the C termini (present in VP8). The following sequence, which contains two sites (indicated with asterisks) and can be cleaved by trypsin was deduced: ... VPVSIVSR*NIVYTR*AQPNQDIVVSKTS....
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0042-6822
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
144
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11-9
pubmed:dateRevised
2009-11-3
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Primary structure of the cleavage site associated with trypsin enhancement of rotavirus SA11 infectivity.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't