5gvq
From Proteopedia
(Difference between revisions)
Line 3: | Line 3: | ||
<StructureSection load='5gvq' size='340' side='right'caption='[[5gvq]]' scene=''> | <StructureSection load='5gvq' size='340' side='right'caption='[[5gvq]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[5gvq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens | + | <table><tr><td colspan='2'>[[5gvq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5GVQ FirstGlance]. <br> |
- | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=5gvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gvq OCA], [https://pdbe.org/5gvq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gvq RCSB], [https://www.ebi.ac.uk/pdbsum/5gvq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gvq ProSAT]</span></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=5gvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gvq OCA], [https://pdbe.org/5gvq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gvq RCSB], [https://www.ebi.ac.uk/pdbsum/5gvq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gvq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Line 11: | Line 11: | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/SF3B4_HUMAN SF3B4_HUMAN] Subunit of the splicing factor SF3B required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex. SF3B4 has been found in complex 'B' and 'C' as well. Belongs also to the minor U12-dependent spliceosome, which is involved in the splicing of rare class of nuclear pre-mRNA intron. | [https://www.uniprot.org/uniprot/SF3B4_HUMAN SF3B4_HUMAN] Subunit of the splicing factor SF3B required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex. SF3B4 has been found in complex 'B' and 'C' as well. Belongs also to the minor U12-dependent spliceosome, which is involved in the splicing of rare class of nuclear pre-mRNA intron. | ||
+ | <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> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 5gvq" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== |
Current revision
Solution structure of the first RRM domain of human spliceosomal protein SF3b49
|
Categories: Homo sapiens | Large Structures | Guntert P | Inoue M | Ito T | Kigawa T | Kobayashi N | Kuwasako K | Muto Y | Nameki N | Sakamoto T | Sato A | Shirouzu M | Takahashi M | Takahashi S | Terada T | Tochio N | Tsuda K | Wakamatsu K | Yokoyama S