4a4f: Difference between revisions
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==Solution structure of SPF30 Tudor domain in complex with symmetrically dimethylated arginine== | |||
<StructureSection load='4a4f' size='340' side='right'caption='[[4a4f]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4a4f]] 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=4A4F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A4F FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2MR:N3,+N4-DIMETHYLARGININE'>2MR</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4a4e|4a4e]], [[4a4g|4a4g]], [[4a4h|4a4h]]</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=4a4f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a4f OCA], [https://pdbe.org/4a4f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a4f RCSB], [https://www.ebi.ac.uk/pdbsum/4a4f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a4f ProSAT]</span></td></tr> | |||
</table> | |||
== 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;"> | |||
== Publication Abstract from PubMed == | |||
Arginine 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<ref>PMID:22101937</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4a4f" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Human]] | |||
[[Category: Large Structures]] | |||
[[Category: Englbrecht, C]] | |||
[[Category: Fessas, D]] | |||
[[Category: Fischer, U]] | |||
[[Category: Machyna, M]] | |||
[[Category: Madl, T]] | |||
[[Category: Neugebauer, K M]] | |||
[[Category: Sattler, M]] | |||
[[Category: Tripsianes, K]] | |||
[[Category: Rna binding protein]] | |||