2bze

<StructureSection load='2bze' size='340' side='right' caption='[[2bze]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[2bze]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BZE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BZE 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=2bze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bze OCA], [http://pdbe.org/2bze PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bze RCSB], [http://www.ebi.ac.uk/pdbsum/2bze PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2bze ProSAT]</span></td></tr>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

The yeast Paf1 complex consists of Paf1, Rtf1, Cdc73, Ctr9, and Leo1 and regulates histone H2B ubiquitination, histone H3 methylation, RNA polymerase II carboxy-terminal domain (CTD) Ser2 phosphorylation, and RNA 3' end processing. We provide structural insight into the Paf1 complex with the NMR structure of the conserved and functionally important Plus3 domain of human Rtf1. A predominantly beta-stranded subdomain displays structural similarity to Dicer/Argonaute PAZ domains and to Tudor domains. We further demonstrate that the highly basic Rtf1 Plus3 domain can interact in vitro with single-stranded DNA via residues on the rim of the beta sheet, reminiscent of siRNA binding by PAZ domains, but did not detect binding to double-stranded DNA or RNA. We discuss the potential role of Rtf1 Plus3 ssDNA binding during transcription elongation.

Structure and DNA binding of the human Rtf1 Plus3 domain.,de Jong RN, Truffault V, Diercks T, Ab E, Daniels MA, Kaptein R, Folkers GE Structure. 2008 Jan;16(1):149-59. PMID:18184592<ref>PMID:18184592</ref>

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

</div>

<div class="pdbe-citations 2bze" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Human]]

[[Category: Ab, E]]

[[Category: Daniels, M A]]

[[Category: Diercks, T]]

[[Category: Folkers, G E]]

[[Category: Jong, R N.De]]

[[Category: Kaptein, R]]

[[Category: SPINE, Structural Proteomics in Europe]]

[[Category: Truffault, V]]

[[Category: Transcription regulation]]