| pubmed-article:7918464 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7918464 | lifeskim:mentions | umls-concept:C0022940 | lld:lifeskim |
| pubmed-article:7918464 | lifeskim:mentions | umls-concept:C0039667 | lld:lifeskim |
| pubmed-article:7918464 | lifeskim:mentions | umls-concept:C0041041 | lld:lifeskim |
| pubmed-article:7918464 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:7918464 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:7918464 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:7918464 | lifeskim:mentions | umls-concept:C0037633 | lld:lifeskim |
| pubmed-article:7918464 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:7918464 | lifeskim:mentions | umls-concept:C2825311 | lld:lifeskim |
| pubmed-article:7918464 | lifeskim:mentions | umls-concept:C1382100 | lld:lifeskim |
| pubmed-article:7918464 | lifeskim:mentions | umls-concept:C2349209 | lld:lifeskim |
| pubmed-article:7918464 | pubmed:issue | 41 | lld:pubmed |
| pubmed-article:7918464 | pubmed:dateCreated | 1994-11-10 | lld:pubmed |
| pubmed-article:7918464 | pubmed:abstractText | Two- and three-dimensional (2D and 3D) NMR techniques have been used to assign the signals from nearly all of the protons in Lactobacillus casei dihydrofolate reductase (DHFR) (M(r) 18,300) in its 1:1 complex with the antibacterial drug trimethoprim. A sample of uniformly 15N-labeled protein was examined using 3D 15N/1H experiments [nuclear Overhauser, heteronuclear multiple quantum coherence (NOESY-HMQC) and total correlation, heteronuclear multiple quantum coherence (TOCSY-HMQC) experiments]. Twenty-two intermolecular NOEs between trimethoprim and protein protons and four intramolecular NOEs in the ligand have been detected. Some were obtained by using heteronuclear editing and 2D HMQC-NOESY experiments on complexes formed with 15N-and 13C-labeled trimethoprim molecules ([1,3-15N2,2-amino-15N]-and [7-13C,4'-methoxy-13C]trimethoprim) bound to unlabeled protein. The ligand-protein NOEs were used as distance constraints in conjunction with minimum energy and simulated annealing calculations (carried out with X-PLOR) to dock the trimethoprim ligand into dihydrofolate reductase, using as a starting structure the crystal coordinates from a related complex with a similar overall protein structure. The restrained minimum energy calculations and the simulated annealing calculations gave 83 calculated structures with distance violations of < 0.1 A. In all of these, the two aromatic rings of trimethoprim occupied essentially the same region of conformational space in the binding site (RMSD = 0.63 A). The protein residues nearest to the bound trimethoprim were found to be very similar in all of the structures and agreed well with corresponding contact residues observed in the X-ray crystal studies on trimethoprim complexes formed with Escherichia coli and chicken liver DHFRs. | lld:pubmed |
| pubmed-article:7918464 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7918464 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7918464 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7918464 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7918464 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7918464 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7918464 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7918464 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7918464 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7918464 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:7918464 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:7918464 | pubmed:author | pubmed-author:FeeneyJJ | lld:pubmed |
| pubmed-article:7918464 | pubmed:author | pubmed-author:BirdsallBB | lld:pubmed |
| pubmed-article:7918464 | pubmed:author | pubmed-author:CheungH THT | lld:pubmed |
| pubmed-article:7918464 | pubmed:author | pubmed-author:BauerC JCJ | lld:pubmed |
| pubmed-article:7918464 | pubmed:author | pubmed-author:FrenkielT ATA | lld:pubmed |
| pubmed-article:7918464 | pubmed:author | pubmed-author:PolshakovV... | lld:pubmed |
| pubmed-article:7918464 | pubmed:author | pubmed-author:KuyperLL | lld:pubmed |
| pubmed-article:7918464 | pubmed:author | pubmed-author:MartorellGG | lld:pubmed |
| pubmed-article:7918464 | pubmed:author | pubmed-author:GradwellM JMJ | lld:pubmed |
| pubmed-article:7918464 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7918464 | pubmed:day | 18 | lld:pubmed |
| pubmed-article:7918464 | pubmed:volume | 33 | lld:pubmed |
| pubmed-article:7918464 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7918464 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7918464 | pubmed:pagination | 12416-26 | lld:pubmed |
| pubmed-article:7918464 | pubmed:dateRevised | 2009-9-29 | lld:pubmed |
| pubmed-article:7918464 | pubmed:meshHeading | pubmed-meshheading:7918464-... | lld:pubmed |
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| pubmed-article:7918464 | pubmed:meshHeading | pubmed-meshheading:7918464-... | lld:pubmed |
| pubmed-article:7918464 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7918464 | pubmed:articleTitle | Solution structure of bound trimethoprim in its complex with Lactobacillus casei dihydrofolate reductase. | lld:pubmed |
| pubmed-article:7918464 | pubmed:affiliation | Laboratory of Molecular Structure, National Institute for Medical Research, Mill Hill, London, U.K. | lld:pubmed |
| pubmed-article:7918464 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7918464 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:7918464 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7918464 | lld:pubmed |
