rdf:type |
|
lifeskim:mentions |
umls-concept:C0017337,
umls-concept:C0086418,
umls-concept:C0597357,
umls-concept:C0679058,
umls-concept:C1514562,
umls-concept:C1517050,
umls-concept:C1547699,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2700400,
umls-concept:C2700640
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pubmed:issue |
8-9
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pubmed:dateCreated |
2000-9-14
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pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/AF215825,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/AF215826,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/AF215827,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/AF215828,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/AF215829,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/AF215830,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/AF215831,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/AF215832,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/AF215833,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/AF215834,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/AF215835
|
pubmed:abstractText |
Human killer-cell immunoglobulin-like receptors (KIR) show three types of organization of their extracellular domains: D0-D1-D2 in KIR3D, D1-D2 in the majority of KIR2D, and D0-D2 in KIR2DL4 and the novel KIR2DL5. The gene for a KIR2DL3 variant, which has a D1-D2 structure, has been shown previously to have a nonexpressed region (pseudoexon 3) that is paralogous to the exon encoding the D0 domain of other KIR. This pseudoexon is not expressed because it is skipped during splicing of pre-mRNA. In this study, we demonstrate that all eight genes encoding human KIR with D1-D2 configuration (KIR2DL1-KIR2DL3, KIR2DS1-KIR2DS5) have similarly untranslated pseudoexons. Whereas the pseudoexons of four of these KIR genes bear nonsense mutations and/or altered splicing sites, the pseudoexons in the other four KIR genes have no major structural abnormalities, indicating that other mechanisms are responsible for inactivation of their exons 3. A comparison of the sequences on pseudoexons 3 with the paralogous expressed exons suggests that an exonic splicing enhancer may be necessary for the expression of exon 3 in KIR genes.
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pubmed:grant |
|
pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/KIR2DL3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/KIR2DL4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, KIR,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, KIR2DL1,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, KIR2DL3,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, KIR2DL4
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
|
pubmed:issn |
0093-7711
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
51
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
639-46
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:10941835-Adult,
pubmed-meshheading:10941835-Base Sequence,
pubmed-meshheading:10941835-DNA, Complementary,
pubmed-meshheading:10941835-Exons,
pubmed-meshheading:10941835-Humans,
pubmed-meshheading:10941835-Killer Cells, Natural,
pubmed-meshheading:10941835-Molecular Sequence Data,
pubmed-meshheading:10941835-Protein Biosynthesis,
pubmed-meshheading:10941835-Protein Structure, Tertiary,
pubmed-meshheading:10941835-Pseudogenes,
pubmed-meshheading:10941835-Receptors, Immunologic,
pubmed-meshheading:10941835-Receptors, KIR,
pubmed-meshheading:10941835-Receptors, KIR2DL1,
pubmed-meshheading:10941835-Receptors, KIR2DL3,
pubmed-meshheading:10941835-Receptors, KIR2DL4,
pubmed-meshheading:10941835-Sequence Homology, Nucleic Acid,
pubmed-meshheading:10941835-Tumor Cells, Cultured
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pubmed:year |
2000
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pubmed:articleTitle |
Genes encoding human killer-cell Ig-like receptors with D1 and D2 extracellular domains all contain untranslated pseudoexons encoding a third Ig-like domain.
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pubmed:affiliation |
Department of Structural Biology, Stanford University School of Medicine, CA 94305, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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