| pubmed-article:17470806 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17470806 | lifeskim:mentions | umls-concept:C0071163 | lld:lifeskim |
| pubmed-article:17470806 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:17470806 | lifeskim:mentions | umls-concept:C0037633 | lld:lifeskim |
| pubmed-article:17470806 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:17470806 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:17470806 | lifeskim:mentions | umls-concept:C1382100 | lld:lifeskim |
| pubmed-article:17470806 | lifeskim:mentions | umls-concept:C1517050 | lld:lifeskim |
| pubmed-article:17470806 | pubmed:issue | 19 | lld:pubmed |
| pubmed-article:17470806 | pubmed:dateCreated | 2007-5-9 | lld:pubmed |
| pubmed-article:17470806 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17470806 | pubmed:abstractText | The pituitary adenylate cyclase-activating polypeptide (PACAP) receptor is a class II G protein-coupled receptor that contributes to many different cellular functions including neurotransmission, neuronal survival, and synaptic plasticity. The solution structure of the potent antagonist PACAP (residues 6'-38') complexed to the N-terminal extracellular (EC) domain of the human splice variant hPAC1-R-short (hPAC1-R(S)) was determined by NMR. The PACAP peptide adopts a helical conformation when bound to hPAC1-R(S) with a bend at residue A18' and makes extensive hydrophobic and electrostatic interactions along the exposed beta-sheet and interconnecting loops of the N-terminal EC domain. Mutagenesis data on both the peptide and the receptor delineate the critical interactions between the C terminus of the peptide and the C terminus of the EC domain that define the high affinity and specificity of hormone binding to hPAC1-R(S). These results present a structural basis for hPAC1-R(S) selectivity for PACAP versus the vasoactive intestinal peptide and also differentiate PACAP residues involved in binding to the N-terminal extracellular domain versus other parts of the full-length hPAC1-R(S) receptor. The structural, mutational, and binding data are consistent with a model for peptide binding in which the C terminus of the peptide hormone interacts almost exclusively with the N-terminal EC domain, whereas the central region makes contacts to both the N-terminal and other extracellular parts of the receptor, ultimately positioning the N terminus of the peptide to contact the transmembrane region and result in receptor activation. | lld:pubmed |
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| pubmed-article:17470806 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17470806 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17470806 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:17470806 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17470806 | pubmed:month | May | lld:pubmed |
| pubmed-article:17470806 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:17470806 | pubmed:author | pubmed-author:OlejniczakEdw... | lld:pubmed |
| pubmed-article:17470806 | pubmed:author | pubmed-author:ScottVictoria... | lld:pubmed |
| pubmed-article:17470806 | pubmed:author | pubmed-author:RichardsonPau... | lld:pubmed |
| pubmed-article:17470806 | pubmed:author | pubmed-author:HajdukPhilip... | lld:pubmed |
| pubmed-article:17470806 | pubmed:author | pubmed-author:SunChaohongC | lld:pubmed |
| pubmed-article:17470806 | pubmed:author | pubmed-author:UchicMarie... | lld:pubmed |
| pubmed-article:17470806 | pubmed:author | pubmed-author:Davis-TaberRa... | lld:pubmed |
| pubmed-article:17470806 | pubmed:author | pubmed-author:SolomonLarry... | lld:pubmed |
| pubmed-article:17470806 | pubmed:author | pubmed-author:BarrettLeo... | lld:pubmed |
| pubmed-article:17470806 | pubmed:author | pubmed-author:WalterKarl... | lld:pubmed |
| pubmed-article:17470806 | pubmed:author | pubmed-author:SongDanyingD | lld:pubmed |
| pubmed-article:17470806 | pubmed:author | pubmed-author:LakeMarc RMR | lld:pubmed |
| pubmed-article:17470806 | pubmed:author | pubmed-author:Pereda-LopezA... | lld:pubmed |
| pubmed-article:17470806 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17470806 | pubmed:day | 8 | lld:pubmed |
| pubmed-article:17470806 | pubmed:volume | 104 | lld:pubmed |
| pubmed-article:17470806 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17470806 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17470806 | pubmed:pagination | 7875-80 | lld:pubmed |
| pubmed-article:17470806 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:17470806 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17470806 | pubmed:articleTitle | Solution structure and mutational analysis of pituitary adenylate cyclase-activating polypeptide binding to the extracellular domain of PAC1-RS. | lld:pubmed |
| pubmed-article:17470806 | pubmed:affiliation | Global Pharmaceutical Discovery Division, Abbott Laboratories, Abbott Park, IL 60064, USA. | lld:pubmed |
| pubmed-article:17470806 | pubmed:publicationType | Journal Article | lld:pubmed |
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