rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
6
|
pubmed:dateCreated |
1995-9-7
|
pubmed:abstractText |
The RNP domain is found in a number of proteins involved in processing and transport of mRNA precursors. The crystal structure of a complex between the U1A spliceosomal protein and its cognate RNA hairpin at 1.92 A resolution reveals the molecular basis of sequence-specific RNA recognition by the RNP domain.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0968-0004
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
20
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
235-40
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:7543225-Amino Acid Sequence,
pubmed-meshheading:7543225-Base Sequence,
pubmed-meshheading:7543225-Biological Transport,
pubmed-meshheading:7543225-Molecular Sequence Data,
pubmed-meshheading:7543225-Protein Structure, Tertiary,
pubmed-meshheading:7543225-RNA,
pubmed-meshheading:7543225-RNA Processing, Post-Transcriptional,
pubmed-meshheading:7543225-RNA-Binding Proteins,
pubmed-meshheading:7543225-Ribonucleoproteins
|
pubmed:year |
1995
|
pubmed:articleTitle |
The RNP domain: a sequence-specific RNA-binding domain involved in processing and transport of RNA.
|
pubmed:affiliation |
MRC Laboratory of Molecular Biology, Cambridge, UK.
|
pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
|