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==Solution structure of the first RRM domain of human spliceosomal protein SF3b49== | |||
<StructureSection load='5gvq' size='340' side='right' caption='[[5gvq]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5gvq]] is a 1 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1x5u 1x5u]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GVQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GVQ FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1x5u|1x5u]]</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5gvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gvq OCA], [http://pdbe.org/5gvq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gvq RCSB], [http://www.ebi.ac.uk/pdbsum/5gvq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gvq ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The spliceosomal protein SF3b49, a component of the splicing factor 3b (SF3b) protein complex in the U2 small nuclear ribonucleoprotein, contains two RNA recognition motif (RRM) domains. In yeast, the first RRM domain (RRM1) of Hsh49 protein (yeast orthologue of human SF3b49) reportedly interacts with another component, Cus1 protein (orthologue of human SF3b145). Here, we solved the solution structure of the RRM1 of human SF3b49 and examined its mode of interaction with a fragment of human SF3b145 using NMR methods. Chemical shift mapping showed that the SF3b145 fragment spanning residues 598-631 interacts with SF3b49 RRM1, which adopts a canonical RRM fold with a topology of beta1-alpha1-beta2-beta3-alpha2-beta4. Furthermore, a docking model based on NOESY measurements suggests that residues 607-616 of the SF3b145 fragment adopt a helical structure that binds to RRM1 predominantly via alpha1, consequently exhibiting a helix-helix interaction in almost antiparallel. This mode of interaction was confirmed by a mutational analysis using GST pull-down assays. Comparison with structures of all RRM domains when complexed with a peptide found that this helix-helix interaction is unique to SF3b49 RRM1. Additionally, all amino acid residues involved in the interaction are well conserved among eukaryotes, suggesting evolutionary conservation of this interaction mode between SF3b49 RRM1 and SF3b145. | |||
Solution structure of the first RNA recognition motif domain of human spliceosomal protein SF3b49 and its mode of interaction with a SF3b145 fragment.,Kuwasako K, Nameki N, Tsuda K, Takahashi M, Sato A, Tochio N, Inoue M, Terada T, Kigawa T, Kobayashi N, Shirouzu M, Ito T, Sakamoto T, Wakamatsu K, Guntert P, Takahashi S, Yokoyama S, Muto Y Protein Sci. 2017 Feb;26(2):280-291. doi: 10.1002/pro.3080. Epub 2016 Nov 27. PMID:27862552<ref>PMID:27862552</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5gvq" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Guntert, P]] | |||
[[Category: Inoue, M]] | |||
[[Category: Ito, T]] | |||
[[Category: Kigawa, T]] | |||
[[Category: Kobayashi, N]] | |||
[[Category: Kuwasako, K]] | |||
[[Category: Muto, Y]] | |||
[[Category: Nameki, N]] | |||
[[Category: Structural genomic]] | |||
[[Category: Sakamoto, T]] | |||
[[Category: Sato, A]] | |||
[[Category: Shirouzu, M]] | |||
[[Category: Takahashi, M]] | |||
[[Category: Takahashi, S]] | |||
[[Category: Terada, T]] | |||
[[Category: Tochio, N]] | |||
[[Category: Tsuda, K]] | |||
[[Category: Wakamatsu, K]] | |||
[[Category: Yokoyama, S]] | |||
[[Category: Rna binding protein]] | |||
[[Category: Rrm]] | |||
[[Category: Rsgi]] | |||
[[Category: Sf3b145]] | |||
[[Category: Sf3b49]] | |||
[[Category: U2 snrnp]] | |||
Revision as of 14:32, 12 April 2017
Solution structure of the first RRM domain of human spliceosomal protein SF3b49Solution structure of the first RRM domain of human spliceosomal protein SF3b49
Structural highlights
Publication Abstract from PubMedThe spliceosomal protein SF3b49, a component of the splicing factor 3b (SF3b) protein complex in the U2 small nuclear ribonucleoprotein, contains two RNA recognition motif (RRM) domains. In yeast, the first RRM domain (RRM1) of Hsh49 protein (yeast orthologue of human SF3b49) reportedly interacts with another component, Cus1 protein (orthologue of human SF3b145). Here, we solved the solution structure of the RRM1 of human SF3b49 and examined its mode of interaction with a fragment of human SF3b145 using NMR methods. Chemical shift mapping showed that the SF3b145 fragment spanning residues 598-631 interacts with SF3b49 RRM1, which adopts a canonical RRM fold with a topology of beta1-alpha1-beta2-beta3-alpha2-beta4. Furthermore, a docking model based on NOESY measurements suggests that residues 607-616 of the SF3b145 fragment adopt a helical structure that binds to RRM1 predominantly via alpha1, consequently exhibiting a helix-helix interaction in almost antiparallel. This mode of interaction was confirmed by a mutational analysis using GST pull-down assays. Comparison with structures of all RRM domains when complexed with a peptide found that this helix-helix interaction is unique to SF3b49 RRM1. Additionally, all amino acid residues involved in the interaction are well conserved among eukaryotes, suggesting evolutionary conservation of this interaction mode between SF3b49 RRM1 and SF3b145. Solution structure of the first RNA recognition motif domain of human spliceosomal protein SF3b49 and its mode of interaction with a SF3b145 fragment.,Kuwasako K, Nameki N, Tsuda K, Takahashi M, Sato A, Tochio N, Inoue M, Terada T, Kigawa T, Kobayashi N, Shirouzu M, Ito T, Sakamoto T, Wakamatsu K, Guntert P, Takahashi S, Yokoyama S, Muto Y Protein Sci. 2017 Feb;26(2):280-291. doi: 10.1002/pro.3080. Epub 2016 Nov 27. PMID:27862552[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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