Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2006-1-11
pubmed:abstractText
The polypyrimidine tract binding protein (PTB) is a 58 kDa protein involved in many aspects of RNA metabolism. In this study, we focused our attention on the structure of the two C-terminal RNA recognition motifs (RRM3 and RRM4) of PTB. In a previous study, it was found that the two RRMs are independent in the free state. We recently determined the structure of the same fragment in complex with RNA and found that the two RRMs interact extensively. This difference made us re-evaluate in detail the free protein structure and in particular the interdomain interface. We used a combination of NMR spectroscopy and segmental isotopic labeling to unambiguously study and characterize the interdomain interactions. An improved segmental isotopic labeling protocol was used, enabling us to unambiguously identify 130 interdomain NOEs between the two RRMs and to calculate a very precise structure. The structure reveals a large interdomain interface, resulting in a very unusual positioning of the two RRM domains relative to one another.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-10207106, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-10217141, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-10231563, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-10323862, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-10334339, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-10373440, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-10407673, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-10499800, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-10856256, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-10982855, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-11003644, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-11036654, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-11175903, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-11313454, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-11445534, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-11457362, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-11552794, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-11726525, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-11788707, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-12084914, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-12522306, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-12578833, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-12626339, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-14739639, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-15039777, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-15116359, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-15121839, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-15341728, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-15853797, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-15908942, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-16179478, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-2690953, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-7543225, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-8756411, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-8972770, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-9164463, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-9214659, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-9299339, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-9367762, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-9377155, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-9436911, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-9618476, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-9632677, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-9646873, http://linkedlifedata.com/resource/pubmed/commentcorrection/16362043-9892643
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0261-4189
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
25
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
150-62
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Structure of the two most C-terminal RNA recognition motifs of PTB using segmental isotope labeling.
pubmed:affiliation
Institute for Molecular Biology and Biophysics, Swiss Federal Institute of Technology Zurich, ETH-Hönggerberg, Zürich, Switzerland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't