| pubmed-article:19339969 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19339969 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
| pubmed-article:19339969 | lifeskim:mentions | umls-concept:C1421544 | lld:lifeskim |
| pubmed-article:19339969 | lifeskim:mentions | umls-concept:C1563691 | lld:lifeskim |
| pubmed-article:19339969 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:19339969 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
| pubmed-article:19339969 | pubmed:issue | 7242 | lld:pubmed |
| pubmed-article:19339969 | pubmed:dateCreated | 2009-5-1 | lld:pubmed |
| pubmed-article:19339969 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19339969 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19339969 | 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. | lld:pubmed |
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| pubmed-article:19339969 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19339969 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19339969 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19339969 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:19339969 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:19339969 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19339969 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:19339969 | pubmed:issn | 1476-4687 | lld:pubmed |
| pubmed-article:19339969 | pubmed:author | pubmed-author:JacksonLaurie... | lld:pubmed |
| pubmed-article:19339969 | pubmed:author | pubmed-author:ChookYuh... | lld:pubmed |
| pubmed-article:19339969 | pubmed:author | pubmed-author:DongXiuhuaX | lld:pubmed |
| pubmed-article:19339969 | pubmed:author | pubmed-author:SüelKatherine... | lld:pubmed |
| pubmed-article:19339969 | pubmed:author | pubmed-author:GuHongmeiH | lld:pubmed |
| pubmed-article:19339969 | pubmed:author | pubmed-author:BiswasAnindit... | lld:pubmed |
| pubmed-article:19339969 | pubmed:author | pubmed-author:MartinezRitaR | lld:pubmed |
| pubmed-article:19339969 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19339969 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:19339969 | pubmed:volume | 458 | lld:pubmed |
| pubmed-article:19339969 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19339969 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19339969 | pubmed:pagination | 1136-41 | lld:pubmed |
| pubmed-article:19339969 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:19339969 | pubmed:meshHeading | pubmed-meshheading:19339969... | lld:pubmed |
| pubmed-article:19339969 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19339969 | pubmed:articleTitle | Structural basis for leucine-rich nuclear export signal recognition by CRM1. | lld:pubmed |
| pubmed-article:19339969 | pubmed:affiliation | Department of Pharmacology, University of Texas Southwestern Medical Center at Dallas, 6001 Forest Park, Dallas, Texas 75390-9041, USA. | lld:pubmed |
| pubmed-article:19339969 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19339969 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:19339969 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:19339969 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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