1f2i: Difference between revisions

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New page: left|200px<br /><applet load="1f2i" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f2i, resolution 2.35Å" /> '''COCRYSTAL STRUCTURE ...
 
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[[Image:1f2i.gif|left|200px]]<br /><applet load="1f2i" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1f2i, resolution 2.35&Aring;" />
'''COCRYSTAL STRUCTURE OF SELECTED ZINC FINGER DIMER BOUND TO DNA'''<br />


==Overview==
==COCRYSTAL STRUCTURE OF SELECTED ZINC FINGER DIMER BOUND TO DNA==
Protein-protein interactions often play a crucial role in stabilizing, protein-DNA complexes and thus facilitate site-specific DNA recognition., We have worked to incorporate such protein-protein contacts into our, design and selection strategies for short peptide extensions that promote, cooperative binding of zinc finger proteins to DNA. We have determined the, crystal structure of one of these fusion protein-DNA complexes. The, selected peptide extension was found to mediate dimerization by reaching, across the dyad axis and contacting a hydrophobic patch on the surface of, the zinc finger bound to the adjacent DNA site. The peptide-zinc finger, protein interactions observed in this structure are similar to those of, some homeodomain heterodimers. We also find that the region of the zinc, finger surface contacted by the selected peptide extension corresponds to, surfaces that also make key interactions in the zinc finger proteins GLI, and SWI5.
<StructureSection load='1f2i' size='340' side='right'caption='[[1f2i]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1f2i]] is a 12 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=1F2I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F2I FirstGlance]. <br>
1F2I 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=1F2I OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</td></tr>
 
<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>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f2i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f2i OCA], [https://pdbe.org/1f2i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f2i RCSB], [https://www.ebi.ac.uk/pdbsum/1f2i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f2i ProSAT]</span></td></tr>
Selected peptide extension contacts hydrophobic patch on neighboring zinc finger and mediates dimerization on DNA., Wang BS, Grant RA, Pabo CO, Nat Struct Biol. 2001 Jul;8(7):589-93. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11427887 11427887]
</table>
== Function ==
[https://www.uniprot.org/uniprot/EGR1_MOUSE EGR1_MOUSE] Transcriptional regulator. Recognizes and binds to the DNA sequence 5'-CGCCCCCGC-3'(EGR-site). Activates the transcription of target genes whose products are required for mitogenesis and differentiation.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f2/1f2i_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1f2i ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Grant RA]]
[[Category: Grant, R.A.]]
[[Category: Pabo CO]]
[[Category: Pabo, C.O.]]
[[Category: Wang BS]]
[[Category: Wang, B.S.]]
[[Category: ZN]]
[[Category: cooperativity]]
[[Category: dimer]]
[[Category: protein-dna complex]]
[[Category: zinc finger]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:32:55 2007''

Latest revision as of 10:09, 7 February 2024

COCRYSTAL STRUCTURE OF SELECTED ZINC FINGER DIMER BOUND TO DNACOCRYSTAL STRUCTURE OF SELECTED ZINC FINGER DIMER BOUND TO DNA

Structural highlights

1f2i is a 12 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.35Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

EGR1_MOUSE Transcriptional regulator. Recognizes and binds to the DNA sequence 5'-CGCCCCCGC-3'(EGR-site). Activates the transcription of target genes whose products are required for mitogenesis and differentiation.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1f2i, resolution 2.35Å

Drag the structure with the mouse to rotate

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OCA
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