1y96: Difference between revisions

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[[Image:1y96.gif|left|200px]]
{{Seed}}
[[Image:1y96.png|left|200px]]


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{{STRUCTURE_1y96|  PDB=1y96  |  SCENE=  }}  
{{STRUCTURE_1y96|  PDB=1y96  |  SCENE=  }}  


'''crystal structure of the Gemin6/Gemin7 heterodimer from the human SMN complex'''
===crystal structure of the Gemin6/Gemin7 heterodimer from the human SMN complex===




==Overview==
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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 line below this paragraph, {{ABSTRACT_PUBMED_15939020}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15939020 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15939020}}


==About this Structure==
==About this Structure==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Sm fold]]
[[Category: Sm fold]]
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