|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
5281
|
|
pubmed:dateCreated |
1996-9-27
|
|
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.
|
|
pubmed:grant |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arginine,
http://linkedlifedata.com/resource/pubmed/chemical/Asparagine,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Gene Products, rev,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Threonine,
http://linkedlifedata.com/resource/pubmed/chemical/rev Gene Products, Human...
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Sep
|
|
pubmed:issn |
0036-8075
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
13
|
|
pubmed:volume |
273
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
1547-51
|
|
pubmed:dateRevised |
2009-11-19
|
|
pubmed:meshHeading |
pubmed-meshheading:8703216-Amino Acid Sequence,
pubmed-meshheading:8703216-Arginine,
pubmed-meshheading:8703216-Asparagine,
pubmed-meshheading:8703216-Base Composition,
pubmed-meshheading:8703216-Base Sequence,
pubmed-meshheading:8703216-DNA-Binding Proteins,
pubmed-meshheading:8703216-Fungal Proteins,
pubmed-meshheading:8703216-Gene Products, rev,
pubmed-meshheading:8703216-Genes, env,
pubmed-meshheading:8703216-HIV-1,
pubmed-meshheading:8703216-Hydrogen Bonding,
pubmed-meshheading:8703216-Magnetic Resonance Spectroscopy,
pubmed-meshheading:8703216-Models, Molecular,
pubmed-meshheading:8703216-Molecular Sequence Data,
pubmed-meshheading:8703216-Nucleic Acid Conformation,
pubmed-meshheading:8703216-Protein Kinases,
pubmed-meshheading:8703216-Protein Structure, Secondary,
pubmed-meshheading:8703216-RNA, Viral,
pubmed-meshheading:8703216-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:8703216-Threonine,
pubmed-meshheading:8703216-rev Gene Products, Human Immunodeficiency Virus
|
|
pubmed:year |
1996
|
|
pubmed:articleTitle |
Alpha helix-RNA major groove recognition in an HIV-1 rev peptide-RRE RNA complex.
|
|
pubmed:affiliation |
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|
