2kz3
From Proteopedia
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| - | [[ | + | ==Backbone 1H, 13C, and 15N Chemical Shift Assignments for human Rad51D from 1 to 83== |
| + | <StructureSection load='2kz3' size='340' side='right' caption='[[2kz3]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2kz3]] 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=2KZ3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KZ3 FirstGlance]. <br> | ||
| + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2kz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kz3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2kz3 RCSB], [http://www.ebi.ac.uk/pdbsum/2kz3 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Rad51D, one of five Rad51 paralogs, is required for homologous recombination and disruption of Holliday junctions with bloom syndrome protein (BLM) in vertebrates. The N-terminal domain of Rad51D is highly conserved in eukaryotic Rad51D orthologs and is essential for protein-protein interaction with XRCC2, but nothing is known about its individual structure or function. In this study, we determined the solution structure of the human Rad51D N-terminal domain (residues 1-83), which consists of four short helices flanked by long N- and C-terminal tails. Interestingly, the position of the N-terminal tail (residues 1-13) is fixed within the domain structure via several hydrophobic interactions between Leu4 and Thr27, Leu4 and Val28, and Val6 and Ile17. We show that the domain preferentially binds to ssDNA versus dsDNA and does not bind to a mobile Holliday junction by electrophoretic mobility shift assay. NMR titration and dynamics studies showed that human Rad51D-N interacts with ssDNA by positively charged and hydrophobic residues on its surface. The results suggest that the N-terminal domain of Rad51D is required for the ssDNA-specific binding function of human Rad51D and that the conserved N-terminal domains of other Rad51 paralogs may have distinguishable functions from each other in homologous recombination. | ||
| - | + | Structural and functional characterization of the N-terminal domain of human Rad51D.,Kim YM, Choi BS Int J Biochem Cell Biol. 2010 Nov 24. PMID:21111057<ref>PMID:21111057</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Choi, N | + | [[Category: Choi, N]] |
| - | [[Category: Kim, Y | + | [[Category: Kim, Y]] |
[[Category: Homologous recombination]] | [[Category: Homologous recombination]] | ||
[[Category: Rad51d]] | [[Category: Rad51d]] | ||
[[Category: Unknown function]] | [[Category: Unknown function]] | ||
Revision as of 08:42, 26 November 2014
Backbone 1H, 13C, and 15N Chemical Shift Assignments for human Rad51D from 1 to 83
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