1gnf

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(New page: 200px<br /><applet load="1gnf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gnf" /> '''SOLUTION STRUCTURE OF THE N-TERMINAL ZINC FI...)
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[[Image:1gnf.gif|left|200px]]<br /><applet load="1gnf" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1gnf" />
 
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'''SOLUTION STRUCTURE OF THE N-TERMINAL ZINC FINGER OF MURINE GATA-1, NMR, 25 STRUCTURES'''<br />
 
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==Overview==
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==SOLUTION STRUCTURE OF THE N-TERMINAL ZINC FINGER OF MURINE GATA-1, NMR, 25 STRUCTURES==
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Zinc fingers (ZnFs) are generally regarded as DNA-binding motifs. However, a number of recent reports have implicated particular ZnFs in the, mediation of protein-protein interactions. The N-terminal ZnF of GATA-1, (NF) is one such finger, having been shown to interact with a number of, other proteins, including the recently discovered transcriptional, co-factor FOG. Here we solve the three-dimensional structure of the NF in, solution using multidimensional 1H/15N NMR spectroscopy, and we use 1H/15N, spin relaxation measurements to investigate its backbone dynamics. The, structure consists of two distorted beta-hairpins and a single, alpha-helix, and is similar to that of the C-terminal ZnF of chicken, GATA-1. Comparisons of the NF structure with those of other C4-type zinc, binding motifs, including hormone receptor and LIM domains, also reveal, substantial structural homology. Finally, we use the structure to map the, spatial locations of NF residues shown by mutagenesis to be essential for, FOG binding, and demonstrate that these residues all lie on a single face, of the NF. Notably, this face is well removed from the putative, DNA-binding face of the NF, an observation which is suggestive of, simultaneous roles for the NF; that is, stabilisation of GATA-1 DNA, complexes and recruitment of FOG to GATA-1-controlled promoter regions.
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<StructureSection load='1gnf' size='340' side='right'caption='[[1gnf]]' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1gnf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GNF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GNF FirstGlance]. <br>
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1GNF 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 ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GNF OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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==Reference==
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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=1gnf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gnf OCA], [https://pdbe.org/1gnf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gnf RCSB], [https://www.ebi.ac.uk/pdbsum/1gnf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gnf ProSAT]</span></td></tr>
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The solution structure of the N-terminal zinc finger of GATA-1 reveals a specific binding face for the transcriptional co-factor FOG., Kowalski K, Czolij R, King GF, Crossley M, Mackay JP, J Biomol NMR. 1999 Mar;13(3):249-62. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10212985 10212985]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GATA1_MOUSE GATA1_MOUSE] Transcriptional activator which probably serves as a general switch factor for erythroid development. It binds to DNA sites with the consensus sequence [AT]GATA[AG] within regulatory regions of globin genes and of other genes expressed in erythroid cells.<ref>PMID:2276623</ref> <ref>PMID:8206977</ref> <ref>PMID:8524811</ref> <ref>PMID:15173587</ref> <ref>PMID:16888089</ref>
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== Evolutionary Conservation ==
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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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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gn/1gnf_consurf.spt"</scriptWhenChecked>
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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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</jmolCheckbox>
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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=1gnf ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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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: Crossley M]]
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[[Category: Crossley, M.]]
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[[Category: Czolij R]]
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[[Category: Czolij, R.]]
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[[Category: King GF]]
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[[Category: King, G.F.]]
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[[Category: Kowalski K]]
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[[Category: Kowalski, K.]]
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[[Category: Mackay JP]]
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[[Category: Mackay, J.P.]]
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[[Category: ZN]]
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[[Category: transcription regulation]]
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[[Category: zinc finger]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:11:07 2007''
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Current revision

SOLUTION STRUCTURE OF THE N-TERMINAL ZINC FINGER OF MURINE GATA-1, NMR, 25 STRUCTURES

PDB ID 1gnf

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