View source for 2ykq


==Structure of the human LINE-1 ORF1p trimer==
<StructureSection load='2ykq' size='340' side='right'caption='[[2ykq]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ykq]] is a 3 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=2YKQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YKQ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=2ykq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ykq OCA], [https://pdbe.org/2ykq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ykq RCSB], [https://www.ebi.ac.uk/pdbsum/2ykq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ykq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LORF1_HUMAN LORF1_HUMAN] Nucleic acid-binding protein which is essential for retrotransposition of LINE-1 elements in the genome. May function as a nucleic acid chaperone binding its own transcript and therefore preferentially mobilizing the transcript from which they are encoded.<ref>PMID:11158327</ref> <ref>PMID:21937507</ref> <ref>PMID:8945518</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The LINE-1 (L1) retrotransposon emerges as a major source of human interindividual genetic variation, with important implications for evolution and disease. L1 retrotransposition is poorly understood at the molecular level, and the mechanistic details and evolutionary origin of the L1-encoded L1ORF1 protein (L1ORF1p) are particularly obscure. Here three crystal structures of trimeric L1ORF1p and NMR solution structures of individual domains reveal a sophisticated and highly structured, yet remarkably flexible, RNA-packaging protein. It trimerizes via an N-terminal, ion-containing coiled coil that serves as scaffold for the flexible attachment of the central RRM and the C-terminal CTD domains. The structures explain the specificity for single-stranded RNA substrates, and a mutational analysis indicates that the precise control of domain flexibility is critical for retrotransposition. Although the evolutionary origin of L1ORF1p remains unclear, our data reveal previously undetected structural and functional parallels to viral proteins.

Trimeric structure and flexibility of the L1ORF1 protein in human L1 retrotransposition.,Khazina E, Truffault V, Buttner R, Schmidt S, Coles M, Weichenrieder O Nat Struct Mol Biol. 2011 Aug 7. doi: 10.1038/nsmb.2097. PMID:21822284<ref>PMID:21822284</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2ykq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Khazina E]]
[[Category: Weichenrieder O]]