1y96

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(New page: 200px<br /> <applet load="1y96" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y96, resolution 2.002&Aring;" /> '''crystal structure ...)
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caption="1y96, resolution 2.002&Aring;" />
caption="1y96, resolution 2.002&Aring;" />
'''crystal structure of the Gemin6/Gemin7 heterodimer from the human SMN complex'''<br />
'''crystal structure of the Gemin6/Gemin7 heterodimer from the human SMN complex'''<br />
==Overview==
==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.
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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.
==About this Structure==
==About this Structure==
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1Y96 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Y96 OCA].
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1Y96 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y96 OCA].
==Reference==
==Reference==
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[[Category: Dostie, J.]]
[[Category: Dostie, J.]]
[[Category: Dreyfuss, G.]]
[[Category: Dreyfuss, G.]]
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[[Category: Duyne, G.D.Van.]]
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[[Category: Duyne, G D.Van.]]
[[Category: Ma, Y.]]
[[Category: Ma, Y.]]
[[Category: protein complex]]
[[Category: protein complex]]
[[Category: sm fold]]
[[Category: sm fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:16:39 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:02:58 2008''

Revision as of 14:02, 21 February 2008


1y96, resolution 2.002Å

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

Overview

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.

About this Structure

1Y96 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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

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