Linked Life Data

7541349

Source:http://linkedlifedata.com/resource/pubmed/id/7541349

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1995-8-9
pubmed:databankReference
pubmed:abstractText
The sequence of the C-terminal 1058 amino acids of atlantic salmon (Salmo salar) apolipoprotein (apo) B was deduced from the nucleotide sequence of cloned cDNA. In comparison with chicken or mammals apoB-100, salmon apoB is C-terminally truncated and extended gaps are found. The two clusters of positively charged residues, previously identified as part of the putative low-density-lipoprotein (LDL) receptor-binding domain of apoB, are brought into close proximity in salmon apoB. This is achieved by the absence between the two clusters of the proline-rich area with the potential to form an amphipathic beta sheet, present in higher vertebrates. In addition, analysis of apoB amino acid sequences currently available in vertebrates revealed the presence of an extended internal duplication in the putative LDL receptor-binding domain. Thus, the two basic clusters would have been duplicated resulting in the presence, except for salmon apoB, of two homologous sites in the C-terminal part of the molecule. The results described here together with earlier biochemical and genetic evidence support the view that Arg3500, a residue mutated in familial defective apoB-100, could be included in a folded critical region of the putative LDL receptor-binding domain of human apoB-100. This region possibly brings the two sub-domains that arise from the duplication close to each other.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
230
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
45-51
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Presence of an extended duplication in the putative low-density-lipoprotein receptor-binding domain of apolipoprotein B. Cloning and characterization of the domain in salmon.
pubmed:affiliation
URA 1134 du Centre National de la Recherche Scientifique, Université Paris-Sud, Orsay, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't