|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
7242
|
|
pubmed:dateCreated |
2009-5-1
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
CRM1 (also known as XPO1 and exportin 1) mediates nuclear export of hundreds of proteins through the recognition of the leucine-rich nuclear export signal (LR-NES). Here we present the 2.9 A structure of CRM1 bound to snurportin 1 (SNUPN). Snurportin 1 binds CRM1 in a bipartite manner by means of an amino-terminal LR-NES and its nucleotide-binding domain. The LR-NES is a combined alpha-helical-extended structure that occupies a hydrophobic groove between two CRM1 outer helices. The LR-NES interface explains the consensus hydrophobic pattern, preference for intervening electronegative residues and inhibition by leptomycin B. The second nuclear export signal epitope is a basic surface on the snurportin 1 nucleotide-binding domain, which binds an acidic patch on CRM1 adjacent to the LR-NES site. Multipartite recognition of individually weak nuclear export signal epitopes may be common to CRM1 substrates, enhancing CRM1 binding beyond the generally low affinity LR-NES. Similar energetic construction is also used in multipartite nuclear localization signals to provide broad substrate specificity and rapid evolution in nuclear transport.
|
|
pubmed:grant |
|
|
pubmed:commentsCorrections |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids, Unsaturated,
http://linkedlifedata.com/resource/pubmed/chemical/Karyopherins,
http://linkedlifedata.com/resource/pubmed/chemical/Leucine,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Export Signals,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoplasmic and Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/exportin 1 protein,
http://linkedlifedata.com/resource/pubmed/chemical/leptomycin B,
http://linkedlifedata.com/resource/pubmed/chemical/snRNP Core Proteins
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Apr
|
|
pubmed:issn |
1476-4687
|
|
pubmed:author |
|
|
pubmed:issnType |
Electronic
|
|
pubmed:day |
30
|
|
pubmed:volume |
458
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
1136-41
|
|
pubmed:dateRevised |
2010-11-18
|
|
pubmed:meshHeading |
pubmed-meshheading:19339969-Active Transport, Cell Nucleus,
pubmed-meshheading:19339969-Crystallography, X-Ray,
pubmed-meshheading:19339969-Epitopes,
pubmed-meshheading:19339969-Fatty Acids, Unsaturated,
pubmed-meshheading:19339969-Humans,
pubmed-meshheading:19339969-Hydrophobic and Hydrophilic Interactions,
pubmed-meshheading:19339969-Karyopherins,
pubmed-meshheading:19339969-Leucine,
pubmed-meshheading:19339969-Models, Molecular,
pubmed-meshheading:19339969-Nuclear Export Signals,
pubmed-meshheading:19339969-Protein Binding,
pubmed-meshheading:19339969-Protein Conformation,
pubmed-meshheading:19339969-Receptors, Cytoplasmic and Nuclear,
pubmed-meshheading:19339969-Structure-Activity Relationship,
pubmed-meshheading:19339969-Substrate Specificity,
pubmed-meshheading:19339969-snRNP Core Proteins
|
|
pubmed:year |
2009
|
|
pubmed:articleTitle |
Structural basis for leucine-rich nuclear export signal recognition by CRM1.
|
|
pubmed:affiliation |
Department of Pharmacology, University of Texas Southwestern Medical Center at Dallas, 6001 Forest Park, Dallas, Texas 75390-9041, USA.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
|
