Abstract:
:When purified dimers of hemagglutinin-neuraminidase molecules released by protease digestion from three strains of human parainfluenza virus 1 were used in crystallization trials, long thin needle crystals formed. Electron microscopic analysis of these needle crystals revealed that they are composed of stacks of triple-stranded helices with each strand of the helix made up of subunits of hemagglutinin-neuraminidase. To our knowledge, this is the first direct demonstration of the assembly of protein subunits into large triple-stranded helices. An understanding of the organization of these triple helices may shed light on the structural properties of the hemagglutinin-neuraminidase molecules that cause them to form these helices.
journal_name
Proc Natl Acad Sci U S Aauthors
Murti KG,Takimoto T,Laver WG,Portner Adoi
10.1073/pnas.90.4.1523subject
Has Abstractpub_date
1993-02-15 00:00:00pages
1523-5issue
4eissn
0027-8424issn
1091-6490journal_volume
90pub_type
杂志文章abstract::A protein of 87 kilodaltons (87 kDa) was previously identified as a major specific substrate for protein kinase C in neuronal and other tissues. We have now studied the effect of protein kinase C-catalyzed phosphorylation of this protein on its association with membranes in isolated nerve terminals (synaptosomes) from...
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journal_title:Proceedings of the National Academy of Sciences of the United States of America
pub_type: 杂志文章
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更新日期:1975-12-01 00:00:00