rdf:type |
|
lifeskim:mentions |
umls-concept:C0205245,
umls-concept:C0439855,
umls-concept:C0733688,
umls-concept:C0936012,
umls-concept:C1314939,
umls-concept:C1514562,
umls-concept:C1521761,
umls-concept:C1522492,
umls-concept:C1819995,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
|
pubmed:issue |
23
|
pubmed:dateCreated |
1999-7-1
|
pubmed:abstractText |
We present biochemical analyses of the regions of the host cell factor (HCF) involved in VP16 complex formation and in the association between the N- and C-terminal domains of HCF itself. We show that the kelch repeat region of HCF (residues 1-380) is sufficient for VP16 complex formation, but that residues C-terminal to the repeats (positions 381-450) interfere with this activity. However, these latter residues are required for the interaction between the N- and C-terminal regions of HCF. The extreme C-terminal region of HCF, corresponding to an area of strong conservation with a Caenorhabditis elegans homologue, is sufficient for interaction with the N-terminal region. These results are discussed with respect to possible differences in the roles of HCF in VP16 activity versus its normal cellular function.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0021-9258
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
4
|
pubmed:volume |
274
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
16437-43
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:10347205-Animals,
pubmed-meshheading:10347205-Binding Sites,
pubmed-meshheading:10347205-Caenorhabditis elegans,
pubmed-meshheading:10347205-Caenorhabditis elegans Proteins,
pubmed-meshheading:10347205-Herpes Simplex Virus Protein Vmw65,
pubmed-meshheading:10347205-Host Cell Factor C1,
pubmed-meshheading:10347205-Humans,
pubmed-meshheading:10347205-Macromolecular Substances,
pubmed-meshheading:10347205-Proteins,
pubmed-meshheading:10347205-Sequence Homology, Amino Acid,
pubmed-meshheading:10347205-Structure-Activity Relationship,
pubmed-meshheading:10347205-Transcription Factors
|
pubmed:year |
1999
|
pubmed:articleTitle |
Analysis of functional domains of the host cell factor involved in VP16 complex formation.
|
pubmed:affiliation |
Marie Curie Research Institute, The Chart, Oxted, Surrey, RH8 0TL, United Kingdom.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|