pubmed-article:16489764 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16489764 | lifeskim:mentions | umls-concept:C0031298 | lld:lifeskim |
pubmed-article:16489764 | lifeskim:mentions | umls-concept:C0452875 | lld:lifeskim |
pubmed-article:16489764 | lifeskim:mentions | umls-concept:C0034800 | lld:lifeskim |
pubmed-article:16489764 | lifeskim:mentions | umls-concept:C0078315 | lld:lifeskim |
pubmed-article:16489764 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:16489764 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:16489764 | lifeskim:mentions | umls-concept:C0126900 | lld:lifeskim |
pubmed-article:16489764 | lifeskim:mentions | umls-concept:C0681828 | lld:lifeskim |
pubmed-article:16489764 | pubmed:issue | 8 | lld:pubmed |
pubmed-article:16489764 | pubmed:dateCreated | 2006-2-21 | lld:pubmed |
pubmed-article:16489764 | pubmed:abstractText | The cell surface receptor for bacteriophage Lambda is LamB (maltoporin). Responsible for phage binding to LamB is the C-terminal part, gpJ, of phage tail protein J. To study the interaction between LamB and gpJ, a chimera protein composed of maltose binding protein (MBP or MalE) connected to the C-terminal part of J (gpJ, amino acids 684-1131) of phage tail protein J of bacteriophage Lambda was expressed in Escherichia coli and purified to homogeneity. The interaction of the MBP-gpJ chimera protein with reconstituted LamB and its mutants LamB Y118G and the loop deletion mutant LamB Delta4+Delta6+Delta9v was studied using planar lipid bilayer membranes on a single-channel and multichannel level. Titration with the MBP-gpJ chimera blocked completely the ion current through reconstituted LamB when it was added to the cis side, the extracellular side of LamB with a half-saturation constant of approximately 6 nM in 1 M KCl. Control experiments with LamB Delta4+Delta6+Delta9v from which all major external loops had been removed showed similar blocking, whereas MBP alone caused no visible effect. Direct conductance measurement with His(6)-gpJ that contained a hexahistidyl tag (His(6) tag) at the N-terminal end of the protein for easy purification revealed no blocking of the ion current, requiring other measurements for the binding constant. However, when maltoporin was preincubated with His-gpJ, MBP-gpJ could not block the channel, which indicated that also His(6)-gpJ bound to the channel. High-molecular mass bands on SDS-PAGE and Western blots, confirming the planar lipid bilayer experiment results, also demonstrated stable complex formation between His(6)-gpJ and LamB or LamB mutants. The results revealed that phage Lambda binding includes not only the extracellular loops. | lld:pubmed |
pubmed-article:16489764 | pubmed:language | eng | lld:pubmed |
pubmed-article:16489764 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16489764 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:16489764 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16489764 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16489764 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16489764 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16489764 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16489764 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16489764 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16489764 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:16489764 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:16489764 | pubmed:month | Feb | lld:pubmed |
pubmed-article:16489764 | pubmed:issn | 0006-2960 | lld:pubmed |
pubmed-article:16489764 | pubmed:author | pubmed-author:BenzRolandR | lld:pubmed |
pubmed-article:16489764 | pubmed:author | pubmed-author:WinterhalterM... | lld:pubmed |
pubmed-article:16489764 | pubmed:author | pubmed-author:BerkaneEmirE | lld:pubmed |
pubmed-article:16489764 | pubmed:author | pubmed-author:CharbitAlainA | lld:pubmed |
pubmed-article:16489764 | pubmed:author | pubmed-author:OrlikFrankF | lld:pubmed |
pubmed-article:16489764 | pubmed:author | pubmed-author:StegmeierJoha... | lld:pubmed |
pubmed-article:16489764 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:16489764 | pubmed:day | 28 | lld:pubmed |
pubmed-article:16489764 | pubmed:volume | 45 | lld:pubmed |
pubmed-article:16489764 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:16489764 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:16489764 | pubmed:pagination | 2708-20 | lld:pubmed |
pubmed-article:16489764 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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pubmed-article:16489764 | pubmed:year | 2006 | lld:pubmed |
pubmed-article:16489764 | pubmed:articleTitle | Interaction of bacteriophage lambda with its cell surface receptor: an in vitro study of binding of the viral tail protein gpJ to LamB (Maltoporin). | lld:pubmed |
pubmed-article:16489764 | pubmed:affiliation | Lehrstuhl für Biotechnologie, Biocenter of the University of Würzburg, Am Hubland, D-97074 Würzburg, Federal Republic of Germany. | lld:pubmed |
pubmed-article:16489764 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:16489764 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:948548 | entrezgene:pubmed | pubmed-article:16489764 | lld:entrezgene |
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