1r4k

<StructureSection load='1r4k' size='340' side='right'caption='[[1r4k]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1r4k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R4K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R4K FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ago1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>

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== Publication Abstract from PubMed ==

The discovery of RNA-mediated gene-silencing pathways, including RNA interference, highlights a fundamental role of short RNAs in eukaryotic gene regulation and antiviral defence. Members of the Dicer and Argonaute protein families are essential components of these RNA-silencing pathways. Notably, these two families possess an evolutionarily conserved PAZ (Piwi/Argonaute/Zwille) domain whose biochemical function is unknown. Here we report the nuclear magnetic resonance solution structure of the PAZ domain from Drosophila melanogaster Argonaute 1 (Ago1). The structure consists of a left-handed, six-stranded beta-barrel capped at one end by two alpha-helices and wrapped on one side by a distinctive appendage, which comprises a long beta-hairpin and a short alpha-helix. Using structural and biochemical analyses, we demonstrate that the PAZ domain binds a 5-nucleotide RNA with 1:1 stoichiometry. We map the RNA-binding surface to the open face of the beta-barrel, which contains amino acids conserved within the PAZ domain family, and we define the 5'-to-3' orientation of single-stranded RNA bound within that site. Furthermore, we show that PAZ domains from different human Argonaute proteins also bind RNA, establishing a conserved function for this domain.

Structure and conserved RNA binding of the PAZ domain.,Yan KS, Yan S, Farooq A, Han A, Zeng L, Zhou MM Nature. 2003 Nov 27;426(6965):468-74. Epub 2003 Nov 16. PMID:14615802<ref>PMID:14615802</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1r4k" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Drome]]

[[Category: Farooq, A]]

[[Category: Han, A]]

[[Category: Yan, K S]]

[[Category: Yan, S]]

[[Category: Zeng, L]]

[[Category: Zhou, M M]]

[[Category: Rna binding protein]]