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1ib2

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[[Image:1ib2.gif|left|200px]]<br /><applet load="1ib2" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ib2.gif|left|200px]]
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caption="1ib2, resolution 1.90&Aring;" />
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'''CRYSTAL STRUCTURE OF A PUMILIO-HOMOLOGY DOMAIN'''<br />
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{{Structure
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|PDB= 1ib2 |SIZE=350|CAPTION= <scene name='initialview01'>1ib2</scene>, resolution 1.90&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF A PUMILIO-HOMOLOGY DOMAIN'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1IB2 is a [[Single protein]] structure of sequence 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=1IB2 OCA].
==Reference==
==Reference==
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Crystal structure of a Pumilio homology domain., Wang X, Zamore PD, Hall TM, Mol Cell. 2001 Apr;7(4):855-65. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11336708 11336708]
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Crystal structure of a Pumilio homology domain., Wang X, Zamore PD, Hall TM, Mol Cell. 2001 Apr;7(4):855-65. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11336708 11336708]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: pumilio-homology domain]]
[[Category: pumilio-homology domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:09:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:47:58 2008''

Revision as of 09:47, 20 March 2008

Image:1ib2.gif


PDB ID 1ib2

Drag the structure with the mouse to rotate
, resolution 1.90Å
Ligands:
Coordinates: save as pdb, mmCIF, xml



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. 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

Page seeded by OCA on Thu Mar 20 11:47:58 2008

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