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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2007-2-7
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pubmed:databankReference |
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pubmed:abstractText |
Heterotrimeric G proteins are molecular switches that relay information intracellularly in response to various extracellular signals. How ligand-activated G protein-coupled receptors act at a distance to exert exchange activity on the Galpha nucleotide binding pocket is poorly understood. Here we describe the synergistic action of two peptides: one from the third intracellular loop of the D2 dopamine receptor (D2N), and a second, Galpha.GDP-binding peptide (KB-752) that mimics the proposed role of Gbetagamma in receptor-promoted nucleotide exchange. The structure of both peptides in complex with Galpha(i1) suggests that conformational changes in the beta3/alpha2 loop and beta6 strand act in concert for efficient nucleotide exchange. Two key residues in the alpha4 helix were found to define a receptor/Galpha(i) coupling specificity determinant.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-10051542,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-10188585,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-10329698,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-10736173,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-10926528,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-11320227,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-11387333,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-11771396,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-11888275,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-12237474,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-12517447,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-12627940,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-14525988,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-15479639,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-15521361,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-15572765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-15747061,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-16210429,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-16485037,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-16554409,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-16892066,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-17053066,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-17060607,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-17139258,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-2137824,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-8072545,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-8383121,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-8994033,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-9069253,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-9398294,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-9405403,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-9665125,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-9705312,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-9757107,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17264214-9891006
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
104
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2001-6
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:17264214-Amino Acid Sequence,
pubmed-meshheading:17264214-Animals,
pubmed-meshheading:17264214-COS Cells,
pubmed-meshheading:17264214-Cercopithecus aethiops,
pubmed-meshheading:17264214-GTP-Binding Protein alpha Subunits, Gi-Go,
pubmed-meshheading:17264214-Humans,
pubmed-meshheading:17264214-Molecular Sequence Data,
pubmed-meshheading:17264214-Nucleotides,
pubmed-meshheading:17264214-Protein Binding,
pubmed-meshheading:17264214-Receptors, G-Protein-Coupled
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pubmed:year |
2007
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pubmed:articleTitle |
Structural basis for nucleotide exchange on G alpha i subunits and receptor coupling specificity.
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pubmed:affiliation |
Department of Pharmacology and UNC Neuroscience Center, School of Medicine, University of North Carolina, Chapel Hill, NC 27599-7365, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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