7prd

<table><tr><td colspan='2'>[[7prd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PRD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PRD FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7prd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7prd OCA], [https://pdbe.org/7prd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7prd RCSB], [https://www.ebi.ac.uk/pdbsum/7prd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7prd ProSAT]</span></td></tr>

== Function ==

[https://www.uniprot.org/uniprot/NRD1_YEAST NRD1_YEAST] Plays a role in sequence-specific regulation of nuclear pre-mRNA abundance.[https://www.uniprot.org/uniprot/NAB3_YEAST NAB3_YEAST] May be required for packaging pre-mRNAs into ribonucleoprotein structures amenable to efficient nuclear RNA processing. Binds to poly(A)+ RNA. Appears to act in the maintenance of CLN3 mRNA levels.<ref>PMID:7476874</ref>

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

== Publication Abstract from PubMed ==

Heterodimerization of RNA binding proteins Nrd1 and Nab3 is essential to communicate the RNA recognition in the nascent transcript with the Nrd1 recognition of the Ser5-phosphorylated Rbp1 C-terminal domain in RNA polymerase II. The structure of a Nrd1-Nab3 chimera reveals the basis of heterodimerization, filling a missing gap in knowledge of this system. The free form of the Nrd1 interaction domain of Nab3 (NRID) forms a multi-state three-helix bundle that is clamped in a single conformation upon complex formation with the Nab3 interaction domain of Nrd1 (NAID). The latter domain forms two long helices that wrap around NRID, resulting in an extensive protein-protein interface that would explain the highly favorable free energy of heterodimerization. Mutagenesis of some conserved hydrophobic residues involved in the heterodimerization leads to temperature-sensitive phenotypes, revealing the importance of this interaction in yeast cell fitness. The Nrd1-Nab3 structure resembles the previously reported Rna14/Rna15 heterodimer structure, which is part of the poly(A)-dependent termination pathway, suggesting that both machineries use similar structural solutions despite they share little sequence homology and are potentially evolutionary divergent.

Structural basis of Nrd1-Nab3 heterodimerization.,Chaves-Arquero B, Martinez-Lumbreras S, Camero S, Santiveri CM, Mirassou Y, Campos-Olivas R, Jimenez MA, Calvo O, Perez-Canadillas JM Life Sci Alliance. 2022 Jan 12;5(4). pii: 5/4/e202101252. doi:, 10.26508/lsa.202101252. Print 2022 Apr. PMID:35022249<ref>PMID:35022249</ref>

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

</div>

<div class="pdbe-citations 7prd" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Saccharomyces cerevisiae]]