Source:http://linkedlifedata.com/resource/pubmed/id/15611256
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2004-12-21
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pubmed:abstractText |
TAP delivers antigenic peptides into the endoplasmic reticulum (ER) that are subsequently bound by MHC class I molecules. TAP consists of two subunits (TAP1 and TAP2), each with a transmembrane (TMD) and a nucleotide-binding (NBD) domain. The two TAP-NBDs have distinct biochemical properties and control different steps during the peptide translocation process. We noted previously that the nonhomologous C-terminal tails of rat TAP1 and TAP2 determine the distinct functions of TAP-NBD1 and -NBD2. To identify the sequence elements responsible for the asymmetrical NBD function, we constructed chimeric rat TAP variants in which we systematically exchanged sequence regions of different length between the two TAP-NBDs. Our fine-mapping studies demonstrate that a nonhomologous region containing the alpha6/beta10-loop in conjunction with the downstream switch region is directly responsible for the functional separation of the TAP-NBDs. The alpha6/beta10-loop determines the nonsynonymous nucleotide binding of NBD1 and NBD2, whereas the switch region seems to play a critical role in regulating the functional cross-talk between the structural domains of TAP. Based on our findings, we postulate that these two sequence elements build a minimal functional unit that controls the asymmetry of the two TAP-NBDs.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0022-1767
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
174
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
328-39
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15611256-ATP-Binding Cassette Transporters,
pubmed-meshheading:15611256-Amino Acid Sequence,
pubmed-meshheading:15611256-Animals,
pubmed-meshheading:15611256-Binding Sites,
pubmed-meshheading:15611256-Blotting, Western,
pubmed-meshheading:15611256-Cell Line, Tumor,
pubmed-meshheading:15611256-Chimera,
pubmed-meshheading:15611256-Flow Cytometry,
pubmed-meshheading:15611256-Histocompatibility Antigens Class I,
pubmed-meshheading:15611256-Humans,
pubmed-meshheading:15611256-Immunoprecipitation,
pubmed-meshheading:15611256-Molecular Sequence Data,
pubmed-meshheading:15611256-Protein Structure, Tertiary,
pubmed-meshheading:15611256-Protein Transport,
pubmed-meshheading:15611256-Rats
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pubmed:year |
2005
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pubmed:articleTitle |
Functional role of C-terminal sequence elements in the transporter associated with antigen processing.
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pubmed:affiliation |
Institute for Genetics, University of Cologne, Zülpicher Strasse 47, 50674 Cologne, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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