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[[Image:1du0.jpg|left|200px]]


{{Structure
==ENGRAILED HOMEODOMAIN Q50A VARIANT DNA COMPLEX==
|PDB= 1du0 |SIZE=350|CAPTION= <scene name='initialview01'>1du0</scene>, resolution 2.00&Aring;
<StructureSection load='1du0' size='340' side='right'caption='[[1du0]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=DA:2&#39;-DEOXYADENOSINE-5&#39;-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2&#39;-DEOXYCYTIDINE-5&#39;-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2&#39;-DEOXYGUANOSINE-5&#39;-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5&#39;-MONOPHOSPHATE'>DT</scene>
<table><tr><td colspan='2'>[[1du0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DU0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DU0 FirstGlance]. <br>
|ACTIVITY=
</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>
|GENE=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1du0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1du0 OCA], [https://pdbe.org/1du0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1du0 RCSB], [https://www.ebi.ac.uk/pdbsum/1du0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1du0 ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=[[1hdd|1HDD]], [[2hdd|2HDD]], [[3hdd|3HDD]]
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1du0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1du0 OCA], [http://www.ebi.ac.uk/pdbsum/1du0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1du0 RCSB]</span>
[https://www.uniprot.org/uniprot/HMEN_DROME HMEN_DROME] This protein specifies the body segmentation pattern. It is required for the development of the central nervous system. Transcriptional regulator that represses activated promoters. Wg signaling operates by inactivating the SGG repression of EN autoactivation.
}}
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
'''ENGRAILED HOMEODOMAIN Q50A VARIANT DNA COMPLEX'''
Check<jmol>
 
  <jmolCheckbox>
 
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/du/1du0_consurf.spt"</scriptWhenChecked>
==Overview==
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
We have determined the crystal structure of a complex containing the engrailed homeodomain Gln50 --&gt; Ala variant (QA50) bound to the wild-type optimal DNA site (TAATTA) at 2.0 A resolution. Biochemical and genetic studies by other groups have suggested that residue 50 is an important determinant of differential DNA-binding specificity among homeodomains (distinguishing among various sites of the general form TAATNN). However, biochemical studies of the QA50 variant had revealed that it binds almost as tightly as the wild-type protein and with only modest changes in specificity. We have now determined the crystal structure of the QA50 variant to help understand the role of residue 50 in site-specific recognition. Our cocrystal structure shows some interesting changes in the water structure at the site of the substitution and shows some changes in the conformations of neighboring side chains. However, the structure, like the QA50 biochemical data, suggests that Gln50 plays a relatively modest role in determining the affinity and specificity of the engrailed homeodomain.
    <text>to colour the structure by Evolutionary Conservation</text>
 
  </jmolCheckbox>
==About this Structure==
</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=1du0 ConSurf].
1DU0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DU0 OCA].  
<div style="clear:both"></div>
 
__TOC__
==Reference==
</StructureSection>
Exploring the role of glutamine 50 in the homeodomain-DNA interface: crystal structure of engrailed (Gln50 --&gt; ala) complex at 2.0 A., Grant RA, Rould MA, Klemm JD, Pabo CO, Biochemistry. 2000 Jul 18;39(28):8187-92. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10889025 10889025]
[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Grant, R A.]]
[[Category: Grant RA]]
[[Category: Klemm, J D.]]
[[Category: Klemm JD]]
[[Category: Pabo, C O.]]
[[Category: Pabo CO]]
[[Category: Rould, M A.]]
[[Category: Rould MA]]
[[Category: dna-binding protein]]
[[Category: homeodomain]]
[[Category: protein-dna complex]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:48:43 2008''

Latest revision as of 09:59, 7 February 2024

ENGRAILED HOMEODOMAIN Q50A VARIANT DNA COMPLEXENGRAILED HOMEODOMAIN Q50A VARIANT DNA COMPLEX

Structural highlights

1du0 is a 4 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HMEN_DROME This protein specifies the body segmentation pattern. It is required for the development of the central nervous system. Transcriptional regulator that represses activated promoters. Wg signaling operates by inactivating the SGG repression of EN autoactivation.

Evolutionary Conservation

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

1du0, resolution 2.00Å

Drag the structure with the mouse to rotate

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OCA
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