View source for 2mmy


==Solution structure of the RNA recognition motif of human TAF15==
<StructureSection load='2mmy' size='340' side='right'caption='[[2mmy]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2mmy]] 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=2MMY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MMY 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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2mmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mmy OCA], [https://pdbe.org/2mmy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mmy RCSB], [https://www.ebi.ac.uk/pdbsum/2mmy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mmy ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/RBP56_HUMAN RBP56_HUMAN] Extraskeletal myxoid chondrosarcoma. A chromosomal aberration involving TAF15/TAF2N is found in a form of extraskeletal myxoid chondrosarcomas (EMC). Translocation t(9;17)(q22;q11) with NR4A3.
== Function ==
[https://www.uniprot.org/uniprot/RBP56_HUMAN RBP56_HUMAN] RNA and ssDNA-binding protein that may play specific roles during transcription initiation at distinct promoters. Can enter the preinitiation complex together with the RNA polymerase II (Pol II).<ref>PMID:19124016</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human TATA binding protein associated factor 2 N (TAF15) and Fused in sarcoma (FUS) are nucleic acid binding proteins belonging to the conserved FET family of proteins. They are involved in diverse processes such as pre-mRNA splicing, mRNA transport, and DNA binding. The absence of information regarding the structural mechanism employed by the FET family in recognizing and discriminating their cognate and non-cognate RNA targets has hampered the attainment of consensus on modes of protein-RNA binding for this family. Our study provides a molecular basis of this RNA recognition using a combination of solution-state NMR spectroscopy, calorimetry, docking and molecular dynamics simulation. Analysis of TAF15-RRM solution structure and its binding with stem-loop RNA has yielded conclusive evidence of a non-canonical mode of RNA recognition. Rather than classical stacking interactions that occur across nitrogen bases and aromatic amino acids on ribonucleoprotein sites, moderate-affinity hydrogen bonding network between the nitrogen bases in the stem-loop RNA and a concave face on the RRM surface primarily mediate TAF15-RRM RNA interaction. We have compared the binding affinities across a set of single-stranded RNA oligonucleotides to conclusively establish that RNA binding is dependent upon structural elements in the RNA rather than sequence.

Structural delineation of stem-loop RNA binding by human TAF15 protein.,Kashyap M, Ganguly AK, Bhavesh NS Sci Rep. 2015 Nov 27;5:17298. doi: 10.1038/srep17298. PMID:26612539<ref>PMID:26612539</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2mmy" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Bhavesh NS]]
[[Category: Ganguly AK]]
[[Category: Kashyap M]]