1du0: Difference between revisions

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OCA

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 <StructureSection load='1du0' size='340' side='right'caption='[[1du0]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1du0]] is a 4 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DU0 FirstGlance]. <br>
+<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>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hdd|1hdd]], [[2hdd|2hdd]], [[3hdd|3hdd]]</td></tr>
+</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1du0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1du0 RCSB], [http://www.ebi.ac.uk/pdbsum/1du0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1du0 ProSAT]</span></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=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>
 </table>
 == Function ==
-[[http://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.
+[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]]
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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=1du0 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-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.
-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:10889025<ref>PMID:10889025</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1du0" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
+[[Category: Drosophila melanogaster]]
 [[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]]
-[[Category: Transcription-dna complex]]