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3uvu
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3uvu is ON HOLD Authors: Barros, A.C., Takeda, A.A.S., Fontes, M.R.M. Description: STRUCTURAL BASIS OF NUCLEAR IMPORT OF FLAP ENDONUCLEASE 1 (FEN1)) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structural basis of nuclear import of Flap endonuclease 1 (FEN1)== | |
| + | <StructureSection load='3uvu' size='340' side='right'caption='[[3uvu]], [[Resolution|resolution]] 2.38Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3uvu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UVU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UVU 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]] 2.38Å</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=3uvu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uvu OCA], [https://pdbe.org/3uvu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uvu RCSB], [https://www.ebi.ac.uk/pdbsum/3uvu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uvu ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FEN1_HUMAN FEN1_HUMAN] Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structurs that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA.<ref>PMID:7961795</ref> <ref>PMID:8621570</ref> <ref>PMID:10744741</ref> <ref>PMID:11986308</ref> <ref>PMID:18443037</ref> <ref>PMID:20729856</ref> | ||
| - | + | ==See Also== | |
| - | + | *[[Importin 3D structures|Importin 3D structures]] | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
| + | [[Category: Barros AC]] | ||
| + | [[Category: Fontes MRM]] | ||
| + | [[Category: Takeda AAS]] | ||
Current revision
Structural basis of nuclear import of Flap endonuclease 1 (FEN1)
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