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1mhn

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(New page: 200px<br /> <applet load="1mhn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mhn, resolution 1.8&Aring;" /> '''High resolution crys...)
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[[Image:1mhn.gif|left|200px]]<br />
 
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<applet load="1mhn" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1mhn, resolution 1.8&Aring;" />
 
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'''High resolution crystal structure of the SMN Tudor domain'''<br />
 
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==Overview==
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==High resolution crystal structure of the SMN Tudor domain==
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The SMN protein, which is linked to spinal muscular atrophy (SMA), plays, an important role in the assembly of the spliceosomal small nuclear, ribonucleoprotein complexes. This function requires binding of SMN to the, arginine-glycine (RG) rich C-terminal tails of the Sm proteins, which, contain symmetrically dimethylated arginine residues (sDMA) in vivo. Using, NMR titrations, we show that the SMN Tudor domain recognizes these sDMAs, in the methylated RG repeats. Upon complex formation a cluster of, conserved aromatic residues in the SMN Tudor domain interacts with the, sDMA methyl groups. We present two high resolution structures of the, uncomplexed SMN Tudor domain, a 1.8A crystal structure and an NMR, structure that has been refined against a large number of backbone and, side-chain residual dipolar couplings. The backbone conformation of both, structures is very similar, however, differences are observed for the, cluster of conserved aromatic side-chains in the sDMA binding pocket. In, order to validate these variations we introduce a novel application of, residual dipolar couplings for aromatic rings. We show that structural, information can be derived from aromatic ring residual dipolar couplings, even in the presence of internal motions such as ring flipping. These, residual dipolar couplings and ring current shifts independently confirm, that the SMN Tudor domain adopts two different conformations in the sDMA, binding pocket. The observed structural variations may play a role for the, recognition of sDMAs.
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<StructureSection load='1mhn' size='340' side='right'caption='[[1mhn]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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==Disease==
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<table><tr><td colspan='2'>[[1mhn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MHN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MHN FirstGlance]. <br>
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Known diseases associated with this structure: Spinal muscular atrophy-1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600354 600354]], Spinal muscular atrophy-2 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600354 600354]], Spinal muscular atrophy-3 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600354 600354]], Spinal muscular atrophy-4 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600354 600354]]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mhn OCA], [https://pdbe.org/1mhn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mhn RCSB], [https://www.ebi.ac.uk/pdbsum/1mhn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mhn ProSAT]</span></td></tr>
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==About this Structure==
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</table>
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1MHN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MHN OCA].
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== Function ==
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[https://www.uniprot.org/uniprot/SMN_HUMAN SMN_HUMAN]
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==Reference==
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== Evolutionary Conservation ==
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High-resolution X-ray and NMR structures of the SMN Tudor domain: conformational variation in the binding site for symmetrically dimethylated arginine residues., Sprangers R, Groves MR, Sinning I, Sattler M, J Mol Biol. 2003 Mar 21;327(2):507-20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12628254 12628254]
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mh/1mhn_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mhn ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Groves, M.R.]]
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[[Category: Groves MR]]
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[[Category: Sattler, M.]]
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[[Category: Sattler M]]
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[[Category: Sinning, I.]]
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[[Category: Sinning I]]
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[[Category: Sprangers, R.]]
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[[Category: Sprangers R]]
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[[Category: sma]]
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[[Category: smn]]
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[[Category: spinal muscular atrophy]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:11:28 2007''
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Current revision

High resolution crystal structure of the SMN Tudor domain

PDB ID 1mhn

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