2kxn

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[[2kxn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KXN OCA]. <br>
[[2kxn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KXN OCA]. <br>
<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
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<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2kxn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kxn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2kxn RCSB], [http://www.ebi.ac.uk/pdbsum/2kxn PDBsum]</span><br>
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Tra2-beta1 is a unique splicing factor as its single RNA recognition motif (RRM) is located between two RS (arginine-serine) domains. To understand how this protein recognizes its RNA target, we solved the structure of Tra2-beta1 RRM in complex with RNA. The central 5'-AGAA-3' motif is specifically recognized by residues from the beta-sheet of the RRM and by residues from both extremities flanking the RRM. The structure suggests that RNA binding by Tra2-beta1 induces positioning of the two RS domains relative to one another. By testing the effect of Tra2-beta1 and RNA mutations on the splicing of SMN2 exon 7, we validated the importance of the RNA-protein contacts observed in the structure for the function of Tra2-beta1 and determined the functional sequence of Tra2-beta1 in SMN2 exon 7. Finally, we propose a model for the assembly of multiple RNA binding proteins on this exon.
Tra2-beta1 is a unique splicing factor as its single RNA recognition motif (RRM) is located between two RS (arginine-serine) domains. To understand how this protein recognizes its RNA target, we solved the structure of Tra2-beta1 RRM in complex with RNA. The central 5'-AGAA-3' motif is specifically recognized by residues from the beta-sheet of the RRM and by residues from both extremities flanking the RRM. The structure suggests that RNA binding by Tra2-beta1 induces positioning of the two RS domains relative to one another. By testing the effect of Tra2-beta1 and RNA mutations on the splicing of SMN2 exon 7, we validated the importance of the RNA-protein contacts observed in the structure for the function of Tra2-beta1 and determined the functional sequence of Tra2-beta1 in SMN2 exon 7. Finally, we propose a model for the assembly of multiple RNA binding proteins on this exon.

Revision as of 10:08, 30 April 2014

NMR structure of human Tra2beta1 RRM in complex with AAGAAC RNA

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