1oai

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

[[https://www.uniprot.org/uniprot/NXF1_HUMAN NXF1_HUMAN]] Involved in the nuclear export of mRNA species bearing retroviral constitutive transport elements (CTE) and in the export of mRNA from the nucleus to the cytoplasm. The NXF1-NXT1 heterodimer is involved in the export of HSP70 mRNA in conjunction with ALYREF/THOC4 and THOC5.<ref>PMID:9660949</ref> <ref>PMID:19165146</ref>

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== Publication Abstract from PubMed ==

The mRNA nuclear export function of Tap/NXF1 requires interactions with nuclear pore proteins (nucleoporins) that contain characteristic Phe-Gly repeats based on FG, GLFG or FxFG cores separated by hydrophilic linkers. FG-nucleoporins bind the two most C-terminal domains of Tap, which have NTF2 and UBA folds, respectively. We used a combination of NMR and X-ray crystallography to define the interaction interface between Tap UBA and FxFG nucleoporins and show that it involves primarily the two aromatic rings of the FxFG core that bind in a hydrophobic surface depression centred on Tap Cys588. NMR evidence indicates that the same depression mediates the binding of GLFG nucleoporins, which we confirmed by demonstrating competition between the two classes of repeat for binding to Tap UBA. Moreover, modification of Cys588 reduced the binding of Tap UBA to both GLFG and FxFG nucleoporins as well as to nuclear envelopes. These data underscore the central role of the conserved FG-nucleoporin repeat cores in binding to Tap UBA and indicate that functional differences between different classes of nucleoporins depend more on their spatial distribution in nuclear pores than on their binding to different sites on Tap UBA.

Structural basis for the interaction between the Tap/NXF1 UBA domain and FG nucleoporins at 1A resolution.,Grant RP, Neuhaus D, Stewart M J Mol Biol. 2003 Feb 21;326(3):849-58. PMID:12581645<ref>PMID:12581645</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 1oai" style="background-color:#fffaf0;"></div>

[[Category: Human]]

[[Category: Grant, R P]]

[[Category: Neuhaus, D]]

[[Category: Stewart, M]]

[[Category: Nucleoporin]]