| pubmed-article:8703216 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8703216 | lifeskim:mentions | umls-concept:C0019704 | lld:lifeskim |
| pubmed-article:8703216 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
| pubmed-article:8703216 | lifeskim:mentions | umls-concept:C0035668 | lld:lifeskim |
| pubmed-article:8703216 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
| pubmed-article:8703216 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:8703216 | lifeskim:mentions | umls-concept:C1518157 | lld:lifeskim |
| pubmed-article:8703216 | pubmed:issue | 5281 | lld:pubmed |
| pubmed-article:8703216 | pubmed:dateCreated | 1996-9-27 | lld:pubmed |
| pubmed-article:8703216 | pubmed:abstractText | The solution structure of a human immunodeficiency virus type-1 (HIV-1) Rev peptide bound to stem-loop IIB of the Rev response element (RRE) RNA was solved by nuclear magnetic resonance spectroscopy. The Rev peptide has an alpha-helical conformation and binds in the major groove of the RNA near a purine-rich internal loop. Several arginine side chains make base-specific contacts, and an asparagine residue contacts a G.A base pair. The phosphate backbone adjacent to a G.G base pair adopts an unusual structure that allows the peptide to access a widened major groove. The structure formed by the two purine-purine base pairs of the RRE creates a distinctive binding pocket that the peptide can use for specific recognition. | lld:pubmed |
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| pubmed-article:8703216 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8703216 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8703216 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8703216 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:8703216 | pubmed:issn | 0036-8075 | lld:pubmed |
| pubmed-article:8703216 | pubmed:author | pubmed-author:WilliamsonJ... | lld:pubmed |
| pubmed-article:8703216 | pubmed:author | pubmed-author:MasLL | lld:pubmed |
| pubmed-article:8703216 | pubmed:author | pubmed-author:TanRR | lld:pubmed |
| pubmed-article:8703216 | pubmed:author | pubmed-author:RaoN SNS | lld:pubmed |
| pubmed-article:8703216 | pubmed:author | pubmed-author:FrankelA DAD | lld:pubmed |
| pubmed-article:8703216 | pubmed:author | pubmed-author:ADIA SAS | lld:pubmed |
| pubmed-article:8703216 | pubmed:author | pubmed-author:MuhandiramD... | lld:pubmed |
| pubmed-article:8703216 | pubmed:author | pubmed-author:BattisteJ LJL | lld:pubmed |
| pubmed-article:8703216 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8703216 | pubmed:day | 13 | lld:pubmed |
| pubmed-article:8703216 | pubmed:volume | 273 | lld:pubmed |
| pubmed-article:8703216 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8703216 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8703216 | pubmed:pagination | 1547-51 | lld:pubmed |
| pubmed-article:8703216 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:8703216 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8703216 | pubmed:articleTitle | Alpha helix-RNA major groove recognition in an HIV-1 rev peptide-RRE RNA complex. | lld:pubmed |
| pubmed-article:8703216 | pubmed:affiliation | Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA. | lld:pubmed |
| pubmed-article:8703216 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8703216 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8703216 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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