4xw3: Difference between revisions
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''' | ==Crystal structure of the SPRY domain of the human DEAD-box protein DDX1== | ||
<StructureSection load='4xw3' size='340' side='right' caption='[[4xw3]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4xw3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XW3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XW3 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=4xw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xw3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xw3 RCSB], [http://www.ebi.ac.uk/pdbsum/4xw3 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The human RNA helicase DDX1 in the DEAD-box family plays an important role in RNA processing and has been associated with HIV-1 replication and tumour progression. Whereas previously described DEAD-box proteins have a structurally conserved core, DDX1 shows a unique structural feature: a large SPRY-domain insertion in its RecA-like consensus fold. SPRY domains are known to function as protein-protein interaction platforms. Here, the crystal structure of the SPRY domain of human DDX1 (hDSPRY) is reported at 2.0 A resolution. The structure reveals two layers of concave, antiparallel beta-sheets that stack onto each other and a third beta-sheet beneath the beta-sandwich. A comparison with SPRY-domain structures from other eukaryotic proteins showed that the general beta-sandwich fold is conserved; however, differences were detected in the loop regions, which were identified in other SPRY domains to be essential for interaction with cognate partners. In contrast, in hDSPRY these loop regions are not strictly conserved across species. Interestingly, though, a conserved patch of positive surface charge is found that may replace the connecting loops as a protein-protein interaction surface. The data presented here comprise the first structural information on DDX1 and provide insights into the unique domain architecture of this DEAD-box protein. By providing the structure of a putative interaction domain of DDX1, this work will serve as a basis for further studies of the interaction network within the hetero-oligomeric complexes of DDX1 and of its recruitment to the HIV-1 Rev protein as a viral replication factor. | |||
Structure of the SPRY domain of the human RNA helicase DDX1, a putative interaction platform within a DEAD-box protein.,Kellner JN, Meinhart A Acta Crystallogr F Struct Biol Commun. 2015 Sep 1;71(Pt 9):1176-88. doi:, 10.1107/S2053230X15013709. Epub 2015 Aug 25. PMID:26323305<ref>PMID:26323305</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
[[Category: Kellner, J | __TOC__ | ||
</StructureSection> | |||
[[Category: Kellner, J N]] | |||
[[Category: Meinhart, A]] | [[Category: Meinhart, A]] | ||
[[Category: Beta-sandwich]] | |||
[[Category: Dead-box protein]] | |||
[[Category: Hydrolase]] | |||
[[Category: Insertion domain]] | |||
[[Category: Spry domain]] | |||
Revision as of 14:15, 9 September 2015
Crystal structure of the SPRY domain of the human DEAD-box protein DDX1Crystal structure of the SPRY domain of the human DEAD-box protein DDX1
Structural highlights
Publication Abstract from PubMedThe human RNA helicase DDX1 in the DEAD-box family plays an important role in RNA processing and has been associated with HIV-1 replication and tumour progression. Whereas previously described DEAD-box proteins have a structurally conserved core, DDX1 shows a unique structural feature: a large SPRY-domain insertion in its RecA-like consensus fold. SPRY domains are known to function as protein-protein interaction platforms. Here, the crystal structure of the SPRY domain of human DDX1 (hDSPRY) is reported at 2.0 A resolution. The structure reveals two layers of concave, antiparallel beta-sheets that stack onto each other and a third beta-sheet beneath the beta-sandwich. A comparison with SPRY-domain structures from other eukaryotic proteins showed that the general beta-sandwich fold is conserved; however, differences were detected in the loop regions, which were identified in other SPRY domains to be essential for interaction with cognate partners. In contrast, in hDSPRY these loop regions are not strictly conserved across species. Interestingly, though, a conserved patch of positive surface charge is found that may replace the connecting loops as a protein-protein interaction surface. The data presented here comprise the first structural information on DDX1 and provide insights into the unique domain architecture of this DEAD-box protein. By providing the structure of a putative interaction domain of DDX1, this work will serve as a basis for further studies of the interaction network within the hetero-oligomeric complexes of DDX1 and of its recruitment to the HIV-1 Rev protein as a viral replication factor. Structure of the SPRY domain of the human RNA helicase DDX1, a putative interaction platform within a DEAD-box protein.,Kellner JN, Meinhart A Acta Crystallogr F Struct Biol Commun. 2015 Sep 1;71(Pt 9):1176-88. doi:, 10.1107/S2053230X15013709. Epub 2015 Aug 25. PMID:26323305[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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