4a4h: Difference between revisions
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==Solution structure of SPF30 Tudor domain in complex with asymmetrically dimethylated arginine== | ==Solution structure of SPF30 Tudor domain in complex with asymmetrically dimethylated arginine== | ||
<StructureSection load='4a4h' size='340' side='right'caption='[[4a4h | <StructureSection load='4a4h' size='340' side='right'caption='[[4a4h]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4a4h]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4a4h]] 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=4A4H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A4H FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DA2:NG,NG-DIMETHYL-L-ARGININE'>DA2</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4a4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a4h OCA], [https://pdbe.org/4a4h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a4h RCSB], [https://www.ebi.ac.uk/pdbsum/4a4h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a4h ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/SPF30_HUMAN SPF30_HUMAN] Necessary for spliceosome assembly. Overexpression causes apoptosis.<ref>PMID:9817934</ref> <ref>PMID:11331595</ref> <ref>PMID:11331295</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 23: | Line 23: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Englbrecht | [[Category: Large Structures]] | ||
[[Category: Fessas | [[Category: Englbrecht C]] | ||
[[Category: Fischer | [[Category: Fessas D]] | ||
[[Category: Machyna | [[Category: Fischer U]] | ||
[[Category: Madl | [[Category: Machyna M]] | ||
[[Category: Neugebauer | [[Category: Madl T]] | ||
[[Category: Sattler | [[Category: Neugebauer KM]] | ||
[[Category: Tripsianes | [[Category: Sattler M]] | ||
[[Category: Tripsianes K]] | |||
Latest revision as of 12:09, 15 November 2023
Solution structure of SPF30 Tudor domain in complex with asymmetrically dimethylated arginineSolution structure of SPF30 Tudor domain in complex with asymmetrically dimethylated arginine
Structural highlights
FunctionSPF30_HUMAN Necessary for spliceosome assembly. Overexpression causes apoptosis.[1] [2] [3] Publication Abstract from PubMedArginine dimethylation plays critical roles in the assembly of ribonucleoprotein complexes in pre-mRNA splicing and piRNA pathways. We report solution structures of SMN and SPF30 Tudor domains bound to symmetric and asymmetric dimethylated arginine (DMA) that is inherent in the RNP complexes. An aromatic cage in the Tudor domain mediates dimethylarginine recognition by electrostatic stabilization through cation-pi interactions. Distinct from extended Tudor domains, dimethylarginine binding by the SMN and SPF30 Tudor domains is independent of proximal residues in the ligand. Yet, enhanced micromolar affinities are obtained by external cooperativity when multiple methylation marks are presented in arginine- and glycine-rich peptide ligands. A hydrogen bond network in the SMN Tudor domain, including Glu134 and a tyrosine hydroxyl of the aromatic cage, enhances cation-pi interactions and is impaired by a mutation causing an E134K substitution associated with spinal muscular atrophy. Our structural analysis enables the design of an optimized binding pocket and the prediction of DMA binding properties of Tudor domains. Structural basis for dimethylarginine recognition by the Tudor domains of human SMN and SPF30 proteins.,Tripsianes K, Madl T, Machyna M, Fessas D, Englbrecht C, Fischer U, Neugebauer KM, Sattler M Nat Struct Mol Biol. 2011 Nov 20. doi: 10.1038/nsmb.2185. PMID:22101937[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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