2fy1

<StructureSection load='2fy1' size='340' side='right'caption='[[2fy1]], [[NMR_Ensembles_of_Models | 17 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[2fy1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FY1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FY1 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=2fy1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fy1 OCA], [https://pdbe.org/2fy1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fy1 RCSB], [https://www.ebi.ac.uk/pdbsum/2fy1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fy1 ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/RBY1A_HUMAN RBY1A_HUMAN]] RNA-binding protein involved in pre-mRNA splicing. Required for sperm development. Acts additively with TRA2B to promote exon 7 inclusion of the survival motor neuron SMN. Binds non-specifically to mRNAs.<ref>PMID:8269511</ref> <ref>PMID:12165565</ref>

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== Publication Abstract from PubMed ==

The RBMY (RNA-binding motif gene on Y chromosome) protein encoded by the human Y chromosome is important for normal sperm development. Although its precise molecular RNA targets are unknown at present, it is suggested that human RBMY (hRBMY) participates in splicing in the testis. Using systematic evolution of ligands by exponential enrichment, we found that RNA stem-loops capped by a C(A)/(U)CAA pentaloop are high-affinity binding targets for hRBMY. Subsequent nuclear magnetic resonance structural determination of the hRBMY RNA recognition motif (RRM) in complex with a high-affinity target showed two distinct modes of RNA recognition. First, the RRM beta-sheet surface binds to the RNA loop in a sequence-specific fashion. Second, the beta2-beta3 loop of the hRBMY inserts into the major groove of the RNA stem. The first binding mode might be conserved in the paralogous protein heterogeneous nuclear RNP G, whereas the second mode of binding is found only in hRBMY. This structural difference could be at the origin of the function of RBMY in spermatogenesis.

The testis-specific human protein RBMY recognizes RNA through a novel mode of interaction.,Skrisovska L, Bourgeois CF, Stefl R, Grellscheid SN, Kister L, Wenter P, Elliott DJ, Stevenin J, Allain FH EMBO Rep. 2007 Apr;8(4):372-9. Epub 2007 Feb 23. PMID:17318228<ref>PMID:17318228</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 2fy1" style="background-color:#fffaf0;"></div>

[[Category: Human]]

[[Category: Allain, F H.T]]

[[Category: Bourgois, C]]

[[Category: Elliot, D]]

[[Category: Kister, L]]

[[Category: Skrisovska, L]]

[[Category: Stefl, R]]

[[Category: Stevenin, J]]

[[Category: Wenter, P]]

[[Category: Structural protein-rna complex]]