Linked Life Data

2050668

Source:http://linkedlifedata.com/resource/pubmed/id/2050668

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
18
pubmed:dateCreated
1991-7-24
pubmed:databankReference
pubmed:abstractText
The structure of the gene encoding a chicken liver receptor, the chicken hepatic lectin, which mediates endocytosis of glycoproteins has been established. The coding sequence is divided into six exons separated by five introns. The first three exons correspond to separate functional domains of the receptor polypeptide (cytoplasmic tail, transmembrane sequence, and extracellular neck region), while the final three exons encode the Ca(2+)-dependent carbohydrate-recognition domain. These results, as well as computer-assisted multiple sequence comparisons, establish this receptor as the evolutionary homolog of the mammalian asialoglycoprotein receptors. It is interesting that the chicken receptor falls into a subfamily of proteins along with the mammalian asialoglycoprotein receptors, since the saccharide-binding specificity of the chicken receptor resembles more closely that of a different set of calcium-dependent animal lectins, which includes the mannose-binding proteins. The portions of the genes encoding the carbohydrate-recognition domains of these proteins lack introns. The results suggest that divergence of intron-containing and intron-lacking carbohydrate-recognition domains preceded shuffling events in which other functional domains were associated with the carbohydrate-recognition domains. This was followed by further divergence, generating a variety of saccharide-binding specificities.
pubmed:grant
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
25
pubmed:volume
266
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11604-9
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:2050668-Amino Acid Sequence, pubmed-meshheading:2050668-Animals, pubmed-meshheading:2050668-Asialoglycoprotein Receptor, pubmed-meshheading:2050668-Base Sequence, pubmed-meshheading:2050668-Biological Evolution, pubmed-meshheading:2050668-Carbohydrate Metabolism, pubmed-meshheading:2050668-Cattle, pubmed-meshheading:2050668-Chickens, pubmed-meshheading:2050668-Dogs, pubmed-meshheading:2050668-Endocytosis, pubmed-meshheading:2050668-Exons, pubmed-meshheading:2050668-Humans, pubmed-meshheading:2050668-Introns, pubmed-meshheading:2050668-Lectins, pubmed-meshheading:2050668-Liver, pubmed-meshheading:2050668-Molecular Sequence Data, pubmed-meshheading:2050668-Multigene Family, pubmed-meshheading:2050668-Rats, pubmed-meshheading:2050668-Receptors, Immunologic, pubmed-meshheading:2050668-Sequence Homology, Nucleic Acid
pubmed:year
1991
pubmed:articleTitle
Evolutionary conservation of intron position in a subfamily of genes encoding carbohydrate-recognition domains.
pubmed:affiliation
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't