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==NMR structure of human restriction factor APOBEC3A== | |||
<StructureSection load='2m65' size='340' side='right' caption='[[2m65]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | |||
=== | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2m65]] 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=2M65 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2M65 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">APOBEC3A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=2m65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m65 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2m65 RCSB], [http://www.ebi.ac.uk/pdbsum/2m65 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Human APOBEC3A is a single-stranded DNA cytidine deaminase that restricts viral pathogens and endogenous retrotransposons, and has a role in the innate immune response. Furthermore, its potential to act as a genomic DNA mutator has implications for a role in carcinogenesis. A deeper understanding of APOBEC3A's deaminase and nucleic acid-binding properties, which is central to its biological activities, has been limited by the lack of structural information. Here we report the nuclear magnetic resonance solution structure of APOBEC3A and show that the critical interface for interaction with single-stranded DNA substrates includes residues extending beyond the catalytic centre. Importantly, by monitoring deaminase activity in real time, we find that A3A displays similar catalytic activity on APOBEC3A-specific TTCA- or A3G-specific CCCA-containing substrates, involving key determinants immediately 5' of the reactive C. Our results afford novel mechanistic insights into APOBEC3A-mediated deamination and provide the structural basis for further molecular studies. | |||
NMR structure of human restriction factor APOBEC3A reveals substrate binding and enzyme specificity.,Byeon IJ, Ahn J, Mitra M, Byeon CH, Hercik K, Hritz J, Charlton LM, Levin JG, Gronenborn AM Nat Commun. 2013;4:1890. doi: 10.1038/ncomms2883. PMID:23695684<ref>PMID:23695684</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: Ahn, J | [[Category: Ahn, J]] | ||
[[Category: Byeon, C | [[Category: Byeon, C]] | ||
[[Category: Byeon, I L | [[Category: Byeon, I L]] | ||
[[Category: Gronenborn, A M | [[Category: Gronenborn, A M]] | ||
[[Category: Antiviral defense]] | [[Category: Antiviral defense]] | ||
[[Category: Apobec3a]] | [[Category: Apobec3a]] | ||
Revision as of 14:42, 18 December 2014
NMR structure of human restriction factor APOBEC3ANMR structure of human restriction factor APOBEC3A
Structural highlights
Publication Abstract from PubMedHuman APOBEC3A is a single-stranded DNA cytidine deaminase that restricts viral pathogens and endogenous retrotransposons, and has a role in the innate immune response. Furthermore, its potential to act as a genomic DNA mutator has implications for a role in carcinogenesis. A deeper understanding of APOBEC3A's deaminase and nucleic acid-binding properties, which is central to its biological activities, has been limited by the lack of structural information. Here we report the nuclear magnetic resonance solution structure of APOBEC3A and show that the critical interface for interaction with single-stranded DNA substrates includes residues extending beyond the catalytic centre. Importantly, by monitoring deaminase activity in real time, we find that A3A displays similar catalytic activity on APOBEC3A-specific TTCA- or A3G-specific CCCA-containing substrates, involving key determinants immediately 5' of the reactive C. Our results afford novel mechanistic insights into APOBEC3A-mediated deamination and provide the structural basis for further molecular studies. NMR structure of human restriction factor APOBEC3A reveals substrate binding and enzyme specificity.,Byeon IJ, Ahn J, Mitra M, Byeon CH, Hercik K, Hritz J, Charlton LM, Levin JG, Gronenborn AM Nat Commun. 2013;4:1890. doi: 10.1038/ncomms2883. PMID:23695684[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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