2qkd

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[[Image:2qkd.jpg|left|200px]]<br /><applet load="2qkd" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2qkd.jpg|left|200px]]
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caption="2qkd, resolution 2.00&Aring;" />
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'''Crystal structure of tandem ZPR1 domains'''<br />
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{{Structure
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|PDB= 2qkd |SIZE=350|CAPTION= <scene name='initialview01'>2qkd</scene>, resolution 2.00&Aring;
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|SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Residue+A+501'>AC1</scene>, <scene name='pdbsite=AC2:Zn+Binding+Site+For+Residue+A+502'>AC2</scene> and <scene name='pdbsite=AC3:Fmt+Binding+Site+For+Residue+A+778'>AC3</scene>
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=FMT:FORMIC ACID'>FMT</scene>
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|ACTIVITY=
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|GENE= Znf259, Zfp259, Zpr1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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}}
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'''Crystal structure of tandem ZPR1 domains'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2QKD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=FMT:'>FMT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Zn+Binding+Site+For+Residue+A+501'>AC1</scene>, <scene name='pdbsite=AC2:Zn+Binding+Site+For+Residue+A+502'>AC2</scene> and <scene name='pdbsite=AC3:Fmt+Binding+Site+For+Residue+A+778'>AC3</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QKD OCA].
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2QKD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QKD OCA].
==Reference==
==Reference==
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Structural insights into the interaction of the evolutionarily conserved ZPR1 domain tandem with eukaryotic EF1A, receptors, and SMN complexes., Mishra AK, Gangwani L, Davis RJ, Lambright DG, Proc Natl Acad Sci U S A. 2007 Aug 28;104(35):13930-5. Epub 2007 Aug 17. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17704259 17704259]
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Structural insights into the interaction of the evolutionarily conserved ZPR1 domain tandem with eukaryotic EF1A, receptors, and SMN complexes., Mishra AK, Gangwani L, Davis RJ, Lambright DG, Proc Natl Acad Sci U S A. 2007 Aug 28;104(35):13930-5. Epub 2007 Aug 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17704259 17704259]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: cell cycle]]
[[Category: cell cycle]]
[[Category: double straded anti-parallel beta helix]]
[[Category: double straded anti-parallel beta helix]]
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[[Category: helical hairpins]]
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[[Category: helical hairpin]]
[[Category: metal binding protein]]
[[Category: metal binding protein]]
[[Category: signaling protein]]
[[Category: signaling protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:40:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:26:47 2008''

Revision as of 16:26, 20 March 2008


PDB ID 2qkd

Drag the structure with the mouse to rotate
, resolution 2.00Å
Sites: , and
Ligands: and
Gene: Znf259, Zfp259, Zpr1 (Mus musculus)
Coordinates: save as pdb, mmCIF, xml



Crystal structure of tandem ZPR1 domains


Overview

Eukaryotic genomes encode a zinc finger protein (ZPR1) with tandem ZPR1 domains. In response to growth stimuli, ZPR1 assembles into complexes with eukaryotic translation elongation factor 1A (eEF1A) and the survival motor neurons protein. To gain insight into the structural mechanisms underlying the essential function of ZPR1 in diverse organisms, we determined the crystal structure of a ZPR1 domain tandem and characterized the interaction with eEF1A. The ZPR1 domain consists of an elongation initiation factor 2-like zinc finger and a double-stranded beta helix with a helical hairpin insertion. ZPR1 binds preferentially to GDP-bound eEF1A but does not directly influence the kinetics of nucleotide exchange or GTP hydrolysis. However, ZPR1 efficiently displaces the exchange factor eEF1Balpha from preformed nucleotide-free complexes, suggesting that it may function as a negative regulator of eEF1A activation. Structure-based mutational and complementation analyses reveal a conserved binding epitope for eEF1A that is required for normal cell growth, proliferation, and cell cycle progression. Structural differences between the ZPR1 domains contribute to the observed functional divergence and provide evidence for distinct modalities of interaction with eEF1A and survival motor neuron complexes.

About this Structure

2QKD is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Structural insights into the interaction of the evolutionarily conserved ZPR1 domain tandem with eukaryotic EF1A, receptors, and SMN complexes., Mishra AK, Gangwani L, Davis RJ, Lambright DG, Proc Natl Acad Sci U S A. 2007 Aug 28;104(35):13930-5. Epub 2007 Aug 17. PMID:17704259

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