1g2f: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: left|200px<br /><applet load="1g2f" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g2f, resolution 2.00Å" /> '''STRUCTURE OF A CYS2H...
 
No edit summary
 
(16 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1g2f.gif|left|200px]]<br /><applet load="1g2f" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1g2f, resolution 2.00&Aring;" />
'''STRUCTURE OF A CYS2HIS2 ZINC FINGER/TATA BOX COMPLEX (TATAZF;CLONE #6)'''<br />


==Overview==
==STRUCTURE OF A CYS2HIS2 ZINC FINGER/TATA BOX COMPLEX (TATAZF;CLONE #6)==
BACKGROUND: Several methods have been developed for creating Cys2His2 zinc, finger proteins that recognize novel DNA sequences, and these proteins may, have important applications in biological research and gene therapy. In, spite of this progress with design/selection methodology, fundamental, questions remain about the principles that govern DNA recognition. One, hypothesis suggests that recognition can be described by a simple set of, rules--essentially a "recognition code"--but careful assessment of this, proposal has been difficult because there have been few structural studies, of selected zinc finger proteins. RESULTS: We report the high-resolution, cocrystal structures of two zinc finger proteins that had been selected, (as variants of Zif268) to recognize a eukaryotic TATA box sequence. The, overall docking arrangement of the fingers within the major groove of the, DNA is similar to that observed in the Zif268 complex. Nevertheless, comparison of Zif268 and the selected variants reveal significant, differences in the pattern of side chain-base interactions. The new, structures also reveal side chain-side chain interactions (both within and, between fingers) that are important in stabilizing the protein-DNA, interface and appear to play substantial roles in recognition., CONCLUSIONS: These new structures highlight the surprising complexity of, zinc finger-DNA interactions. The diversity of interactions observed at, the protein-DNA interface, which is especially striking for proteins that, were all derived from Zif268, challenges fundamental concepts about zinc, finger-DNA recognition and underscores the difficulty in developing any, meaningful recognition code.
<StructureSection load='1g2f' size='340' side='right'caption='[[1g2f]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1g2f]] is a 6 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=1G2F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G2F FirstGlance]. <br>
1G2F 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=1G2F 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&#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=1g2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g2f OCA], [https://pdbe.org/1g2f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g2f RCSB], [https://www.ebi.ac.uk/pdbsum/1g2f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g2f ProSAT]</span></td></tr>
Beyond the "recognition code": structures of two Cys2His2 zinc finger/TATA box complexes., Wolfe SA, Grant RA, Elrod-Erickson M, Pabo CO, Structure. 2001 Aug;9(8):717-23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11587646 11587646]
</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/g2/1g2f_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=1g2f ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Elrod-Erickson M]]
[[Category: Elrod-Erickson, M.]]
[[Category: Grant RA]]
[[Category: Grant, R.A.]]
[[Category: Pabo CO]]
[[Category: Pabo, C.O.]]
[[Category: Wolfe SA]]
[[Category: Wolfe, S.A.]]
[[Category: ZN]]
[[Category: cys2his2]]
[[Category: phage display]]
[[Category: tata box]]
[[Category: zinc finger-dna complex]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:38:40 2007''

Latest revision as of 10:22, 7 February 2024

STRUCTURE OF A CYS2HIS2 ZINC FINGER/TATA BOX COMPLEX (TATAZF;CLONE #6)STRUCTURE OF A CYS2HIS2 ZINC FINGER/TATA BOX COMPLEX (TATAZF;CLONE #6)

Structural highlights

1g2f is a 6 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 2Å
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.

1g2f, resolution 2.00Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1g2f&oldid=4044005"