2b6g: Difference between revisions
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2b6g ConSurf]. | ||
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Revision as of 09:35, 8 February 2016
RNA recognition by the Vts1 SAM domainRNA recognition by the Vts1 SAM domain
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe putative yeast post-transcriptional regulator Vts1p and its related protein Smaug, from Drosophila melanogaster, each use a sterile alpha motif (SAM) domain to bind an RNA hairpin termed the Smaug recognition element (SRE). Here, we present the NMR structures of the Vts1p-SRE complex and the free SRE. Structural highlights include the direct recognition of a guanine base and the formation or stabilization of a base pair in the SRE loop. RNA recognition by the Vts1p SAM domain.,Johnson PE, Donaldson LW Nat Struct Mol Biol. 2006 Feb;13(2):177-8. Epub 2006 Jan 22. PMID:16429155[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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