6brg: Difference between revisions
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The | ==The SAM domain of mouse SAMHD1 is critical for its activation and regulation== | ||
<StructureSection load='6brg' size='340' side='right' caption='[[6brg]], [[Resolution|resolution]] 3.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6brg]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BRG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BRG FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=6brg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6brg OCA], [http://pdbe.org/6brg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6brg RCSB], [http://www.ebi.ac.uk/pdbsum/6brg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6brg ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Human SAMHD1 (hSAMHD1) is a retroviral restriction factor that blocks HIV-1 infection by depleting the cellular nucleotides required for viral reverse transcription. SAMHD1 is allosterically activated by nucleotides that induce assembly of the active tetramer. Although the catalytic core of hSAMHD1 has been studied extensively, previous structures have not captured the regulatory SAM domain. Here we report the crystal structure of full-length SAMHD1 by capturing mouse SAMHD1 (mSAMHD1) structures in three different nucleotide bound states. Although mSAMHD1 and hSAMHD1 are highly similar in sequence and function, we find that mSAMHD1 possesses a more complex nucleotide-induced activation process, highlighting the regulatory role of the SAM domain. Our results provide insights into the regulation of SAMHD1 activity, thereby facilitating the improvement of HIV mouse models and the development of new therapies for certain cancers and autoimmune diseases. | |||
The SAM domain of mouse SAMHD1 is critical for its activation and regulation.,Buzovetsky O, Tang C, Knecht KM, Antonucci JM, Wu L, Ji X, Xiong Y Nat Commun. 2018 Jan 29;9(1):411. doi: 10.1038/s41467-017-02783-8. PMID:29379009<ref>PMID:29379009</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: Antonucci, J | <div class="pdbe-citations 6brg" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Antonucci, J M]] | |||
[[Category: Buzovetsky, O]] | |||
[[Category: Ji, X]] | [[Category: Ji, X]] | ||
[[Category: Knecht, K M]] | |||
[[Category: Tang, C]] | [[Category: Tang, C]] | ||
[[Category: | [[Category: Wu, L]] | ||
[[Category: | [[Category: Xiong, Y]] | ||
[[Category: Allosteric regulation]] | |||
[[Category: Binding site]] | |||
[[Category: Dntpase]] | |||
[[Category: Hydrolase]] | |||
[[Category: Model]] | |||
[[Category: Molecular]] | |||
[[Category: Mouse]] | |||
[[Category: Protein conformation]] | |||
[[Category: Protein multimerization]] | |||
Revision as of 09:33, 15 February 2018
The SAM domain of mouse SAMHD1 is critical for its activation and regulationThe SAM domain of mouse SAMHD1 is critical for its activation and regulation
Structural highlights
Publication Abstract from PubMedHuman SAMHD1 (hSAMHD1) is a retroviral restriction factor that blocks HIV-1 infection by depleting the cellular nucleotides required for viral reverse transcription. SAMHD1 is allosterically activated by nucleotides that induce assembly of the active tetramer. Although the catalytic core of hSAMHD1 has been studied extensively, previous structures have not captured the regulatory SAM domain. Here we report the crystal structure of full-length SAMHD1 by capturing mouse SAMHD1 (mSAMHD1) structures in three different nucleotide bound states. Although mSAMHD1 and hSAMHD1 are highly similar in sequence and function, we find that mSAMHD1 possesses a more complex nucleotide-induced activation process, highlighting the regulatory role of the SAM domain. Our results provide insights into the regulation of SAMHD1 activity, thereby facilitating the improvement of HIV mouse models and the development of new therapies for certain cancers and autoimmune diseases. The SAM domain of mouse SAMHD1 is critical for its activation and regulation.,Buzovetsky O, Tang C, Knecht KM, Antonucci JM, Wu L, Ji X, Xiong Y Nat Commun. 2018 Jan 29;9(1):411. doi: 10.1038/s41467-017-02783-8. PMID:29379009[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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