3mmy

<StructureSection load='3mmy' size='340' side='right' caption='[[3mmy]], [[Resolution|resolution]] 1.65&Aring;' scene=''>

<table><tr><td colspan='2'>[[3mmy]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MMY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MMY FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RAE1, MRNP41 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), NUP98, ADAR2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3mmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mmy OCA], [http://pdbe.org/3mmy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mmy RCSB], [http://www.ebi.ac.uk/pdbsum/3mmy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mmy ProSAT]</span></td></tr>

== Disease ==

[[http://www.uniprot.org/uniprot/NUP98_HUMAN NUP98_HUMAN]] Note=A chromosomal aberration involving NUP98 is found in a form of acute myeloid leukemia. Translocation t(7;11)(p15;p15) with HOXA9. Translocation t(11;17)(p15;p13) with PHF23. Note=A chromosomal aberration involving NUP98 is found in childhood acute myeloid leukemia. Translocation t(5;11)(q35;p15.5) with NSD1. Translocation t(8;11)(p11.2;p15) with WHSC1L1. Note=A chromosomal aberration involving NUP98 is found in a form of therapy-related myelodysplastic syndrome. Translocation t(11;20)(p15;q11) with TOP1. Note=A chromosomal aberration involving NUP98 is found in a form of T-cell acute lymphoblastic leukemia (T-ALL). Translocation t(3;11)(q12.2;p15.4) with LNP1. Note=A chromosomal aberration involving NUP98 is associated with pediatric acute myeloid leukemia (AML) with intermediate characteristics between M2-M3 French-American-British (FAB) subtypes. Translocation t(9;11)(p22;p15) with PSIP1/LEDGF. The chimeric transcript is an in-frame fusion of NUP98 exon 8 to PSIP1/LEDGF exon 4.

[[http://www.uniprot.org/uniprot/RAE1L_HUMAN RAE1L_HUMAN]] Binds mRNA. May function in nucleocytoplasmic transport and in directly or indirectly attaching cytoplasmic mRNPs to the cytoskeleton. [[http://www.uniprot.org/uniprot/NUP98_HUMAN NUP98_HUMAN]] Nup98 and Nup96 play a role in the bidirectional transport across the nucleoporin complex (NPC). The FG repeat domains in Nup98 have a direct role in the transport.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mm/3mmy_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

The export of mRNAs is a multistep process, involving the packaging of mRNAs into messenger ribonucleoprotein particles (mRNPs), their transport through nuclear pore complexes, and mRNP remodeling events prior to translation. Ribonucleic acid export 1 (Rae1) and Nup98 are evolutionarily conserved mRNA export factors that are targeted by the vesicular stomatitis virus matrix protein to inhibit host cell nuclear export. Here, we present the crystal structure of human Rae1 in complex with the Gle2-binding sequence (GLEBS) of Nup98 at 1.65 A resolution. Rae1 forms a seven-bladed beta-propeller with several extensive surface loops. The Nup98 GLEBS motif forms an approximately 50-A-long hairpin that binds with its C-terminal arm to an essentially invariant hydrophobic surface that extends over the entire top face of the Rae1 beta-propeller. The C-terminal arm of the GLEBS hairpin is necessary and sufficient for Rae1 binding, and we identify a tandem glutamate element in this arm as critical for complex formation. The Rae1*Nup98(GLEBS) surface features an additional conserved patch with a positive electrostatic potential, and we demonstrate that the complex possesses single-stranded RNA-binding capability. Together, these data suggest that the Rae1*Nup98 complex directly binds to the mRNP at several stages of the mRNA export pathway.

Structural and functional analysis of the interaction between the nucleoporin Nup98 and the mRNA export factor Rae1.,Ren Y, Seo HS, Blobel G, Hoelz A Proc Natl Acad Sci U S A. 2010 Jun 8;107(23):10406-11. Epub 2010 May 24. PMID:20498086<ref>PMID:20498086</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 3mmy" style="background-color:#fffaf0;"></div>

*[[Nucleoporin|Nucleoporin]]

[[Category: Human]]

[[Category: Hoelz, A]]

[[Category: Ren, Y]]

[[Category: Mrna export]]

[[Category: Nuclear protein]]