1gnf

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[[Image:1gnf.gif|left|200px]]
 
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{{Structure
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==SOLUTION STRUCTURE OF THE N-TERMINAL ZINC FINGER OF MURINE GATA-1, NMR, 25 STRUCTURES==
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|PDB= 1gnf |SIZE=350|CAPTION= <scene name='initialview01'>1gnf</scene>
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<StructureSection load='1gnf' size='340' side='right'caption='[[1gnf]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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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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|ACTIVITY=
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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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|GENE=
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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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|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=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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|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=1gnf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gnf OCA], [http://www.ebi.ac.uk/pdbsum/1gnf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gnf RCSB]</span>
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== Function ==
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}}
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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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'''SOLUTION STRUCTURE OF THE N-TERMINAL ZINC FINGER OF MURINE GATA-1, NMR, 25 STRUCTURES'''
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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/gn/1gnf_consurf.spt"</scriptWhenChecked>
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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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<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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1GNF 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=1GNF 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=1gnf ConSurf].
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<div style="clear:both"></div>
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==Reference==
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== References ==
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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://www.ncbi.nlm.nih.gov/pubmed/10212985 10212985]
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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: transcription regulation]]
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[[Category: zinc finger]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:47:33 2008''
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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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