1m8z
From Proteopedia
(New page: 200px<br /> <applet load="1m8z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m8z, resolution 1.9Å" /> '''Crystal Structure Of...) |
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| - | [[Image:1m8z.gif|left|200px]]<br /> | + | [[Image:1m8z.gif|left|200px]]<br /><applet load="1m8z" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1m8z" size=" | + | |
caption="1m8z, resolution 1.9Å" /> | caption="1m8z, resolution 1.9Å" /> | ||
'''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== | ||
| - | 1M8Z 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]. This structure | + | 1M8Z 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]. This structure supersedes the now removed PDB entry 1IB3. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M8Z 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 domain]] | [[Category: puf domain]] | ||
[[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 13:52:47 2008'' |
Revision as of 11:52, 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
1M8Z is a Single protein structure of sequence from Homo sapiens with as ligand. This structure supersedes the now removed PDB entry 1IB3. 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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