| pubmed-article:9632684 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9632684 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:9632684 | lifeskim:mentions | umls-concept:C0024485 | lld:lifeskim |
| pubmed-article:9632684 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:9632684 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:9632684 | lifeskim:mentions | umls-concept:C0443172 | lld:lifeskim |
| pubmed-article:9632684 | lifeskim:mentions | umls-concept:C0360641 | lld:lifeskim |
| pubmed-article:9632684 | lifeskim:mentions | umls-concept:C0172633 | lld:lifeskim |
| pubmed-article:9632684 | lifeskim:mentions | umls-concept:C0204514 | lld:lifeskim |
| pubmed-article:9632684 | pubmed:issue | 26 | lld:pubmed |
| pubmed-article:9632684 | pubmed:dateCreated | 1998-8-3 | lld:pubmed |
| pubmed-article:9632684 | pubmed:abstractText | The apo- and metal-bound solution conformations of synthetic conantokin-G (con-G, G1Egamma gammaL5Q gamma NQgamma 10LIRgamma K15SN-CONH2, gamma = gamma-carboxyglutamic acid), an antagonist of N-methyl-D-aspartate receptor-derived neuronal ion channels, have been examined by one- and two-dimensional 1H NMR at neutral pH. A complete structure for the Mg2+-loaded peptide was defined by use of distance geometry calculations and was found to exist as an alpha-helix that spans the entire peptide. The alpha-helical nature of Mg2+/con-G was also supported by the small values (<5.5 Hz) of the 3JHNalpha coupling constants measured for amino acid residues 3-5, 8, 9, and 11-16, and the small values (<4 ppb/K) of the temperature coefficients observed for the alphaNH protons of residues 5-17. This conformation contrasted with that obtained for apo-con-G, which was nearly structureless in solution. Docking of Mg2+ into con-G was accomplished by use of the genetic algorithm/molecular dynamics simulation method, employing the NMR-derived Mg2+-loaded structure for initial coordinates in the midpoint calculations. For the 3 Mg2+/con-G model, it was found that binding of one Mg2+ ion is stabilized by oxygen atoms from three gamma-carboxylates of Gla3, Gla4, and Gla7; another Mg2+ is coordinated by two oxygen atoms, one from each of the gamma-carboxylates of Gla7; and a third metal ion through three donor oxygen atoms of gamma-carboxylates from Gla10 and Gla14. As shown from direct metal binding measurements to mutant con-G peptides, these latter two Gla residues probably stabilized the tightest binding Mg2+ ion. Circular dichroism studies of these same peptide variants demonstrated that all Gla residues contribute to the adoption of the Mg2+-dependent alpha-helical conformation in con-G. The data obtained in this investigation provide a molecular basis for the large conformational alteration observed in apo-con-G as a result of divalent cation binding and allow assessment of the roles of individual Gla residues in defining certain of the structure-function properties of con-G. | lld:pubmed |
| pubmed-article:9632684 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9632684 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9632684 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9632684 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9632684 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9632684 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9632684 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9632684 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9632684 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9632684 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9632684 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9632684 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9632684 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9632684 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9632684 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:9632684 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:9632684 | pubmed:author | pubmed-author:CastellinoF... | lld:pubmed |
| pubmed-article:9632684 | pubmed:author | pubmed-author:ChefRR | lld:pubmed |
| pubmed-article:9632684 | pubmed:author | pubmed-author:LORR | lld:pubmed |
| pubmed-article:9632684 | pubmed:author | pubmed-author:PedersenL GLG | lld:pubmed |
| pubmed-article:9632684 | pubmed:author | pubmed-author:ZinAA | lld:pubmed |
| pubmed-article:9632684 | pubmed:author | pubmed-author:ProrokMM | lld:pubmed |
| pubmed-article:9632684 | pubmed:author | pubmed-author:BlancoHH | lld:pubmed |
| pubmed-article:9632684 | pubmed:author | pubmed-author:OEKK | lld:pubmed |
| pubmed-article:9632684 | pubmed:author | pubmed-author:WarderS ESE | lld:pubmed |
| pubmed-article:9632684 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9632684 | pubmed:day | 26 | lld:pubmed |
| pubmed-article:9632684 | pubmed:volume | 273 | lld:pubmed |
| pubmed-article:9632684 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9632684 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9632684 | pubmed:pagination | 16248-58 | lld:pubmed |
| pubmed-article:9632684 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:9632684 | pubmed:meshHeading | pubmed-meshheading:9632684-... | lld:pubmed |
| pubmed-article:9632684 | pubmed:meshHeading | pubmed-meshheading:9632684-... | lld:pubmed |
| pubmed-article:9632684 | pubmed:meshHeading | pubmed-meshheading:9632684-... | lld:pubmed |
| pubmed-article:9632684 | pubmed:meshHeading | pubmed-meshheading:9632684-... | lld:pubmed |
| pubmed-article:9632684 | pubmed:meshHeading | pubmed-meshheading:9632684-... | lld:pubmed |
| pubmed-article:9632684 | pubmed:meshHeading | pubmed-meshheading:9632684-... | lld:pubmed |
| pubmed-article:9632684 | pubmed:meshHeading | pubmed-meshheading:9632684-... | lld:pubmed |
| pubmed-article:9632684 | pubmed:meshHeading | pubmed-meshheading:9632684-... | lld:pubmed |
| pubmed-article:9632684 | pubmed:meshHeading | pubmed-meshheading:9632684-... | lld:pubmed |
| pubmed-article:9632684 | pubmed:meshHeading | pubmed-meshheading:9632684-... | lld:pubmed |
| pubmed-article:9632684 | pubmed:meshHeading | pubmed-meshheading:9632684-... | lld:pubmed |
| pubmed-article:9632684 | pubmed:meshHeading | pubmed-meshheading:9632684-... | lld:pubmed |
| pubmed-article:9632684 | pubmed:meshHeading | pubmed-meshheading:9632684-... | lld:pubmed |
| pubmed-article:9632684 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9632684 | pubmed:articleTitle | Conformational changes in conantokin-G induced upon binding of calcium and magnesium as revealed by NMR structural analysis. | lld:pubmed |
| pubmed-article:9632684 | pubmed:affiliation | Biomolecular NMR Laboratory and the Montreal Joint Center for Structural Biology, Biotechnology Research Institute, National Research Council of Canada, Montreal, Quebec H4P 2R2, Canada. | lld:pubmed |
| pubmed-article:9632684 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9632684 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9632684 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9632684 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9632684 | lld:pubmed |
