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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4302
|
| pubmed:dateCreated |
1977-9-2
|
| pubmed:abstractText |
A central eight-stranded beta-pleated sheet is the main feature of the polypeptide backbone folding in dihydrofolate reductase. The innermost four strands and two bridging helices are geometrically similar to but are connected in a different way from those in the dinucleotide binding domains found in nicotinamide-adenine dinucleotide-linked dehydrogenases. Methotrexate is bound in a 15-angstrom-deep cavity with the pteridine ring buried in a primarily hydrophobic pocket, although a strong interaction occurs between the side chain of aspartic acid 27 and N(1), N(8), and the 2-amino group of methotrexate.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jul
|
| pubmed:issn |
0036-8075
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
29
|
| pubmed:volume |
197
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
452-5
|
| pubmed:dateRevised |
2009-10-27
|
| pubmed:meshHeading |
pubmed-meshheading:17920-Binding Sites,
pubmed-meshheading:17920-Escherichia coli,
pubmed-meshheading:17920-Folic Acid Antagonists,
pubmed-meshheading:17920-Methotrexate,
pubmed-meshheading:17920-Molecular Conformation,
pubmed-meshheading:17920-NADP,
pubmed-meshheading:17920-Protein Conformation,
pubmed-meshheading:17920-Tetrahydrofolate Dehydrogenase,
pubmed-meshheading:17920-X-Ray Diffraction
|
| pubmed:year |
1977
|
| pubmed:articleTitle |
Dihydrofolate reductase: x-ray structure of the binary complex with methotrexate.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
|