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| | ==Solution structure of the RMM-CTD domains of human LINE-1 ORF1p== | | ==Solution structure of the RMM-CTD domains of human LINE-1 ORF1p== |
| - | <StructureSection load='2ldy' size='340' side='right' caption='[[2ldy]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''> | + | <StructureSection load='2ldy' size='340' side='right'caption='[[2ldy]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ldy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LDY OCA]. <br> | + | <table><tr><td colspan='2'>[[2ldy]] 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=2LDY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LDY FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2yko|2yko]], [[2ykp|2ykp]], [[2ykq|2ykq]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></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=2ldy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ldy OCA], [https://pdbe.org/2ldy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ldy RCSB], [https://www.ebi.ac.uk/pdbsum/2ldy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ldy ProSAT]</span></td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ldy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ldy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ldy RCSB], [http://www.ebi.ac.uk/pdbsum/2ldy PDBsum]</span></td></tr> | + | </table> |
| - | <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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | 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> | | 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> |
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 2ldy" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| - | [[Category: Coles, M.]] | + | [[Category: Large Structures]] |
| - | [[Category: Truffault, V.]] | + | [[Category: Coles M]] |
| - | [[Category: Genome evolution]] | + | [[Category: Truffault V]] |
| - | [[Category: Nucleic acid chaperone]]
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| - | [[Category: Rna binding protein]]
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| Structural highlights
Function
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.[1] [2] [3]
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[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wei W, Gilbert N, Ooi SL, Lawler JF, Ostertag EM, Kazazian HH, Boeke JD, Moran JV. Human L1 retrotransposition: cis preference versus trans complementation. Mol Cell Biol. 2001 Feb;21(4):1429-39. PMID:11158327 doi:http://dx.doi.org/10.1128/MCB.21.4.1429-1439.2001
- ↑ Callahan KE, Hickman AB, Jones CE, Ghirlando R, Furano AV. Polymerization and nucleic acid-binding properties of human L1 ORF1 protein. Nucleic Acids Res. 2012 Jan;40(2):813-27. doi: 10.1093/nar/gkr728. Epub 2011 Sep , 21. PMID:21937507 doi:http://dx.doi.org/10.1093/nar/gkr728
- ↑ Moran JV, Holmes SE, Naas TP, DeBerardinis RJ, Boeke JD, Kazazian HH Jr. High frequency retrotransposition in cultured mammalian cells. Cell. 1996 Nov 29;87(5):917-27. PMID:8945518
- ↑ Khazina E, Truffault V, Buttner R, Schmidt S, Coles M, Weichenrieder O. Trimeric structure and flexibility of the L1ORF1 protein in human L1 retrotransposition. Nat Struct Mol Biol. 2011 Aug 7. doi: 10.1038/nsmb.2097. PMID:21822284 doi:10.1038/nsmb.2097
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