View source for 2rrb


==Refinement of RNA binding domain in human Tra2 beta protein==
<StructureSection load='2rrb' size='340' side='right'caption='[[2rrb]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2rrb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RRB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RRB FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2rra|2rra]]</div></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2rrb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rrb OCA], [https://pdbe.org/2rrb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rrb RCSB], [https://www.ebi.ac.uk/pdbsum/2rrb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rrb ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Human Transformer2-beta (hTra2-beta) is an important member of the serine/arginine-rich protein family, and contains one RNA recognition motif (RRM). It controls the alternative splicing of several pre-mRNAs, including those of the calcitonin/calcitonin gene-related peptide (CGRP), the survival motor neuron 1 (SMN1) protein and the tau protein. Accordingly, the RRM of hTra2-beta specifically binds to two types of RNA sequences [the CAA and (GAA)(2) sequences]. We determined the solution structure of the hTra2-beta RRM (spanning residues Asn110-Thr201), which not only has a canonical RRM fold, but also an unusual alignment of the aromatic amino acids on the beta-sheet surface. We then solved the complex structure of the hTra2-beta RRM with the (GAA)(2) sequence, and found that the AGAA tetra-nucleotide was specifically recognized through hydrogen-bond formation with several amino acids on the N- and C-terminal extensions, as well as stacking interactions mediated by the unusually aligned aromatic rings on the beta-sheet surface. Further NMR experiments revealed that the hTra2-beta RRM recognizes the CAA sequence when it is integrated in the stem-loop structure. This study indicates that the hTra2-beta RRM recognizes two types of RNA sequences in different RNA binding modes.

Structural basis for the dual RNA-recognition modes of human Tra2-beta RRM.,Tsuda K, Someya T, Kuwasako K, Takahashi M, He F, Unzai S, Inoue M, Harada T, Watanabe S, Terada T, Kobayashi N, Shirouzu M, Kigawa T, Tanaka A, Sugano S, Guntert P, Yokoyama S, Muto Y Nucleic Acids Res. 2011 Mar;39(4):1538-53. Epub 2010 Oct 5. PMID:20926394<ref>PMID:20926394</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2rrb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Inoue, M]]
[[Category: Kigawa, T]]
[[Category: Kuwasako, K]]
[[Category: Muto, Y]]
[[Category: Structural genomic]]
[[Category: Shirouzu, M]]
[[Category: Someya, T]]
[[Category: Sugano, S]]
[[Category: Takahashi, M]]
[[Category: Terada, T]]
[[Category: Tsuda, K]]
[[Category: Yokoyama, S]]
[[Category: National project on protein structural and functional analyse]]
[[Category: Nppsfa]]
[[Category: Rbd]]
[[Category: Rna binding protein]]
[[Category: Rrm domain]]
[[Category: Rsgi]]