1hdd: Difference between revisions

New page: left|200px<br /><applet load="1hdd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hdd, resolution 2.800Å" /> '''CRYSTAL STRUCTURE O...
 
No edit summary
 
(16 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1hdd.jpg|left|200px]]<br /><applet load="1hdd" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1hdd, resolution 2.800&Aring;" />
'''CRYSTAL STRUCTURE OF AN ENGRAILED HOMEODOMAIN-DNA COMPLEX AT 2.8 ANGSTROMS RESOLUTION: A FRAMEWORK FOR UNDERSTANDING HOMEODOMAIN-DNA INTERACTIONS'''<br />


==Overview==
==CRYSTAL STRUCTURE OF AN ENGRAILED HOMEODOMAIN-DNA COMPLEX AT 2.8 ANGSTROMS RESOLUTION: A FRAMEWORK FOR UNDERSTANDING HOMEODOMAIN-DNA INTERACTIONS==
The crystal structure of a complex containing the engrailed homeodomain, and a duplex DNA site has been determined at 2.8 A resolution and refined, to a crystallographic R factor of 24.4%. In this complex, two separate, regions of the 61 amino acid polypeptide contact a TAAT subsite. An, N-terminal arm fits into the minor groove, and the side chains of Arg-3, and Arg-5 make contacts near the 5' end of this "core consensus" binding, site. An alpha helix fits into the major groove, and the side chains of, IIe-47 and Asn-51 contact base pairs near the 3' end of the TAAT site., This "recognition helix" is part of a structurally conserved, helix-turn-helix unit, but these helices are longer than the corresponding, helices in the lambda repressor, and the relationship between the, helix-turn-helix unit and the DNA is significantly different.
<StructureSection load='1hdd' size='340' side='right'caption='[[1hdd]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1hdd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HDD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HDD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hdd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hdd OCA], [https://pdbe.org/1hdd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hdd RCSB], [https://www.ebi.ac.uk/pdbsum/1hdd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hdd ProSAT]</span></td></tr>
</table>
== Function ==
[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]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hd/1hdd_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=1hdd ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of a complex containing the engrailed homeodomain and a duplex DNA site has been determined at 2.8 A resolution and refined to a crystallographic R factor of 24.4%. In this complex, two separate regions of the 61 amino acid polypeptide contact a TAAT subsite. An N-terminal arm fits into the minor groove, and the side chains of Arg-3 and Arg-5 make contacts near the 5' end of this "core consensus" binding site. An alpha helix fits into the major groove, and the side chains of IIe-47 and Asn-51 contact base pairs near the 3' end of the TAAT site. This "recognition helix" is part of a structurally conserved helix-turn-helix unit, but these helices are longer than the corresponding helices in the lambda repressor, and the relationship between the helix-turn-helix unit and the DNA is significantly different.


==About this Structure==
Crystal structure of an engrailed homeodomain-DNA complex at 2.8 A resolution: a framework for understanding homeodomain-DNA interactions.,Kissinger CR, Liu BS, Martin-Blanco E, Kornberg TB, Pabo CO Cell. 1990 Nov 2;63(3):579-90. PMID:1977522<ref>PMID:1977522</ref>
1HDD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HDD OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystal structure of an engrailed homeodomain-DNA complex at 2.8 A resolution: a framework for understanding homeodomain-DNA interactions., Kissinger CR, Liu BS, Martin-Blanco E, Kornberg TB, Pabo CO, Cell. 1990 Nov 2;63(3):579-90. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1977522 1977522]
</div>
<div class="pdbe-citations 1hdd" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Kissinger, C.R.]]
[[Category: Synthetic construct]]
[[Category: Liu, B.]]
[[Category: Kissinger CR]]
[[Category: Martin-Blanco, E.]]
[[Category: Kornberg TB]]
[[Category: Pabo, T.B.Kornberg C.O.]]
[[Category: Liu B]]
[[Category: double helix]]
[[Category: Martin-Blanco E]]
[[Category: protein-dna complex]]
[[Category: Pabo CO]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:32:03 2007''

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

OCA