1oxj: Difference between revisions
New page: left|200px<br /><applet load="1oxj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oxj, resolution 1.8Å" /> '''Crystal structure of ... |
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[[Image:1oxj.jpg|left|200px]]<br /><applet load="1oxj" size=" | [[Image:1oxj.jpg|left|200px]]<br /><applet load="1oxj" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1oxj, resolution 1.8Å" /> | caption="1oxj, resolution 1.8Å" /> | ||
'''Crystal structure of the Smaug RNA binding domain'''<br /> | '''Crystal structure of the Smaug RNA binding domain'''<br /> | ||
==Overview== | ==Overview== | ||
The Nanos protein gradient in Drosophila, required for proper abdominal | The Nanos protein gradient in Drosophila, required for proper abdominal segmentation, is generated in part via translational repression of its mRNA by Smaug. We report here the crystal structure of the Smaug RNA binding domain, which shows no sequence homology to any previously characterized RNA binding motif. The structure reveals an unusual makeup in which a SAM domain, a common protein-protein interaction module, is affixed to a pseudo-HEAT repeat analogous topology (PHAT) domain. Unexpectedly, we find through a combination of structural and genetic analysis that it is primarily the SAM domain that interacts specifically with the appropriate nanos mRNA regulatory sequence. Therefore, in addition to their previously characterized roles in protein-protein interactions, some SAM domains play crucial roles in RNA binding. | ||
==About this Structure== | ==About this Structure== | ||
1OXJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http:// | 1OXJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OXJ OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Aggarwal, A | [[Category: Aggarwal, A K.]] | ||
[[Category: Gardner, C | [[Category: Gardner, C D.]] | ||
[[Category: Green, J | [[Category: Green, J B.]] | ||
[[Category: Wharton, R | [[Category: Wharton, R P.]] | ||
[[Category: phat domain]] | [[Category: phat domain]] | ||
[[Category: rna-binding protein]] | [[Category: rna-binding protein]] | ||
[[Category: sam domain]] | [[Category: sam domain]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:22:45 2008'' | ||
Revision as of 15:22, 21 February 2008
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Crystal structure of the Smaug RNA binding domain
OverviewOverview
The Nanos protein gradient in Drosophila, required for proper abdominal segmentation, is generated in part via translational repression of its mRNA by Smaug. We report here the crystal structure of the Smaug RNA binding domain, which shows no sequence homology to any previously characterized RNA binding motif. The structure reveals an unusual makeup in which a SAM domain, a common protein-protein interaction module, is affixed to a pseudo-HEAT repeat analogous topology (PHAT) domain. Unexpectedly, we find through a combination of structural and genetic analysis that it is primarily the SAM domain that interacts specifically with the appropriate nanos mRNA regulatory sequence. Therefore, in addition to their previously characterized roles in protein-protein interactions, some SAM domains play crucial roles in RNA binding.
About this StructureAbout this Structure
1OXJ is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
ReferenceReference
RNA recognition via the SAM domain of Smaug., Green JB, Gardner CD, Wharton RP, Aggarwal AK, Mol Cell. 2003 Jun;11(6):1537-48. PMID:12820967
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