1y96

<table><tr><td colspan='2'>[[1y96]] is a 4 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=1Y96 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Y96 FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GEMIN6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), GEMIN7 ([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://proteopedia.org/fgij/fg.htm?mol=1y96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y96 OCA], [http://pdbe.org/1y96 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y96 RCSB], [http://www.ebi.ac.uk/pdbsum/1y96 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1y96 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/GEMI6_HUMAN GEMI6_HUMAN]] The SMN complex plays an essential role in spliceosomal snRNP assembly in the cytoplasm and is required for pre-mRNA splicing in the nucleus.<ref>PMID:11748230</ref> [[http://www.uniprot.org/uniprot/GEMI7_HUMAN GEMI7_HUMAN]] The SMN complex plays an essential role in spliceosomal snRNP assembly in the cytoplasm and is required for pre-mRNA splicing in the nucleus.<ref>PMID:12065586</ref>

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== Publication Abstract from PubMed ==

The survival of motor neurons (SMN) protein, product of the disease gene of the common neurodegenerative disease spinal muscular atrophy, is part of the large multiprotein "SMN complex." The SMN complex functions as an assembly machine for small nuclear ribonucleoproteins (snRNPs)-the major components of the spliceosome. Here, we report the crystal structure of two components of the human SMN complex, Gemin6 and Gemin7. Although Gemin6 and Gemin7 have no significant sequence similarity with Sm proteins, both adopt canonical Sm folds. Moreover, Gemin6 and Gemin7 exist as a heterodimer, and interact with each other via an interface similar to that which mediates interactions among the Sm proteins. Together with binding experiments that show that the Gemin6/Gemin7 complex binds to Sm proteins, these findings provide a framework for considering how the SMN complex, with Gemin6 and Gemin7 as tools, might organize Sm proteins for formation of Sm rings on snRNA targets.

The Gemin6-Gemin7 heterodimer from the survival of motor neurons complex has an Sm protein-like structure.,Ma Y, Dostie J, Dreyfuss G, Van Duyne GD Structure. 2005 Jun;13(6):883-92. PMID:15939020<ref>PMID:15939020</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 1y96" style="background-color:#fffaf0;"></div>

[[Category: Human]]

[[Category: Dostie, J]]

[[Category: Dreyfuss, G]]

[[Category: Duyne, G D.Van]]

[[Category: Ma, Y]]

[[Category: Protein complex]]

[[Category: Sm fold]]