1ib2
From Proteopedia
(New page: 200px<br /> <applet load="1ib2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ib2, resolution 1.90Å" /> '''CRYSTAL STRUCTURE O...) |
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| - | [[Image:1ib2.gif|left|200px]]<br /> | + | [[Image:1ib2.gif|left|200px]]<br /><applet load="1ib2" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ib2" size=" | + | |
caption="1ib2, resolution 1.90Å" /> | caption="1ib2, resolution 1.90Å" /> | ||
'''CRYSTAL STRUCTURE OF A PUMILIO-HOMOLOGY DOMAIN'''<br /> | '''CRYSTAL STRUCTURE OF A PUMILIO-HOMOLOGY DOMAIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Puf proteins regulate translation and mRNA stability by binding sequences | + | Puf proteins regulate translation and mRNA stability by binding sequences in their target RNAs through the Pumilio homology domain (PUM-HD), which is characterized by eight tandem copies of a 36 amino acid motif, the PUM repeat. We have solved the structure of the PUM-HD from human Pumilio1 at 1.9 A resolution. The structure reveals that the eight PUM repeats correspond to eight copies of a single, repeated structural motif. The PUM repeats pack together to form a right-handed superhelix that approximates a half doughnut. The distribution of side chains on the inner and outer faces of this half doughnut suggests that the inner face of the PUM-HD binds RNA while the outer face interacts with proteins such as Nanos, Brain Tumor, and cytoplasmic polyadenylation element binding protein. |
==About this Structure== | ==About this Structure== | ||
| - | 1IB2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with BME as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1IB2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=BME:'>BME</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IB2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Hall, T | + | [[Category: Hall, T M.T.]] |
[[Category: Wang, X.]] | [[Category: Wang, X.]] | ||
| - | [[Category: Zamore, P | + | [[Category: Zamore, P D.]] |
[[Category: BME]] | [[Category: BME]] | ||
[[Category: puf motif]] | [[Category: puf motif]] | ||
[[Category: pumilio-homology domain]] | [[Category: pumilio-homology domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:09:59 2008'' |
Revision as of 11:10, 21 February 2008
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CRYSTAL STRUCTURE OF A PUMILIO-HOMOLOGY DOMAIN
Overview
Puf proteins regulate translation and mRNA stability by binding sequences in their target RNAs through the Pumilio homology domain (PUM-HD), which is characterized by eight tandem copies of a 36 amino acid motif, the PUM repeat. We have solved the structure of the PUM-HD from human Pumilio1 at 1.9 A resolution. The structure reveals that the eight PUM repeats correspond to eight copies of a single, repeated structural motif. The PUM repeats pack together to form a right-handed superhelix that approximates a half doughnut. The distribution of side chains on the inner and outer faces of this half doughnut suggests that the inner face of the PUM-HD binds RNA while the outer face interacts with proteins such as Nanos, Brain Tumor, and cytoplasmic polyadenylation element binding protein.
About this Structure
1IB2 is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of a Pumilio homology domain., Wang X, Zamore PD, Hall TM, Mol Cell. 2001 Apr;7(4):855-65. PMID:11336708
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