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2qkd

From Proteopedia

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[[Image:2qkd.jpg|left|200px]]
 
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{{Structure
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==Crystal structure of tandem ZPR1 domains==
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|PDB= 2qkd |SIZE=350|CAPTION= <scene name='initialview01'>2qkd</scene>, resolution 2.00&Aring;
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<StructureSection load='2qkd' size='340' side='right'caption='[[2qkd]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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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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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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<table><tr><td colspan='2'>[[2qkd]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QKD FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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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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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qkd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qkd OCA], [https://pdbe.org/2qkd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qkd RCSB], [https://www.ebi.ac.uk/pdbsum/2qkd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qkd ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qkd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qkd OCA], [http://www.ebi.ac.uk/pdbsum/2qkd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qkd RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/ZPR1_MOUSE ZPR1_MOUSE] May be a signaling molecule that communicates mitogenic signals from the cytoplasm to the nucleus.
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== Evolutionary Conservation ==
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'''Crystal structure of tandem ZPR1 domains'''
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qk/2qkd_consurf.spt"</scriptWhenChecked>
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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.
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==About this Structure==
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</jmolCheckbox>
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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].
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2qkd ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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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]
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Mishra AK]]
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[[Category: Mishra, A K.]]
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[[Category: anti-parrallel beta sheet]]
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[[Category: beta helix]]
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[[Category: cell cycle]]
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[[Category: double straded anti-parallel beta helix]]
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[[Category: helical hairpin]]
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[[Category: metal binding protein]]
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[[Category: signaling protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:50:15 2008''
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Current revision

Crystal structure of tandem ZPR1 domains

PDB ID 2qkd

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