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2r5z

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Revision as of 11:14, 5 September 2018

Structure of Scr/Exd complex bound to a DNA sequence derived from the fkh gene

Structural highlights

2r5z is a 4 chain structure with sequence from Drome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1b8i, 2r5y
Gene:	Scr (DROME), exd (DROME)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[EXD_DROME] Transcription factor which acts with the selector homeodomain proteins altering the regulation of downstream target genes such as wingless (wg), teashirt (tsh) and decapentaplegic (dpp), thus affecting segmental identity. Delimits the eye field and prevent inappropriate eye development. Required for proper localization of chordotonal organs within the peripheral nervous system.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] [SCR_DROME] Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Controls the segmental transformation of the first to the second thoracic segment (prothorax to mesothorax) and of the labial palps into maxillary palps. In embryo, required for fusion of labial lobes and development of the T1 denticle belt. In adult, expression in the head is necessary for proper development of the labium. In the first thoracic segment of the adult, required for proper development of the sex comb and to suppress improper prothoracic wing development.^[7]

Evolutionary Conservation

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

Publication Abstract from PubMed

The recognition of specific DNA-binding sites by transcription factors is a critical yet poorly understood step in the control of gene expression. Members of the Hox family of transcription factors bind DNA by making nearly identical major groove contacts via the recognition helices of their homeodomains. In vivo specificity, however, often depends on extended and unstructured regions that link Hox homeodomains to a DNA-bound cofactor, Extradenticle (Exd). Using a combination of structure determination, computational analysis, and in vitro and in vivo assays, we show that Hox proteins recognize specific Hox-Exd binding sites via residues located in these extended regions that insert into the minor groove but only when presented with the correct DNA sequence. Our results suggest that these residues, which are conserved in a paralog-specific manner, confer specificity by recognizing a sequence-dependent DNA structure instead of directly reading a specific DNA sequence.

Functional specificity of a Hox protein mediated by the recognition of minor groove structure.,Joshi R, Passner JM, Rohs R, Jain R, Sosinsky A, Crickmore MA, Jacob V, Aggarwal AK, Honig B, Mann RS Cell. 2007 Nov 2;131(3):530-43. PMID:17981120^[8]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Rauskolb C, Peifer M, Wieschaus E. extradenticle, a regulator of homeotic gene activity, is a homolog of the homeobox-containing human proto-oncogene pbx1. Cell. 1993 Sep 24;74(6):1101-12. PMID:8104703
↑ Flegel WA, Singson AW, Margolis JS, Bang AG, Posakony JW, Murre C. Dpbx, a new homeobox gene closely related to the human proto-oncogene pbx1 molecular structure and developmental expression. Mech Dev. 1993 May;41(2-3):155-61. PMID:8100142
↑ Rauskolb C, Wieschaus E. Coordinate regulation of downstream genes by extradenticle and the homeotic selector proteins. EMBO J. 1994 Aug 1;13(15):3561-9. PMID:7914871
↑ Rieckhof GE, Casares F, Ryoo HD, Abu-Shaar M, Mann RS. Nuclear translocation of extradenticle requires homothorax, which encodes an extradenticle-related homeodomain protein. Cell. 1997 Oct 17;91(2):171-83. PMID:9346235
↑ Kurant E, Pai CY, Sharf R, Halachmi N, Sun YH, Salzberg A. Dorsotonals/homothorax, the Drosophila homologue of meis1, interacts with extradenticle in patterning of the embryonic PNS. Development. 1998 Mar;125(6):1037-48. PMID:9463350
↑ Pai CY, Kuo TS, Jaw TJ, Kurant E, Chen CT, Bessarab DA, Salzberg A, Sun YH. The Homothorax homeoprotein activates the nuclear localization of another homeoprotein, extradenticle, and suppresses eye development in Drosophila. Genes Dev. 1998 Feb 1;12(3):435-46. PMID:9450936
↑ Pattatucci AM, Otteson DC, Kaufman TC. A functional and structural analysis of the Sex combs reduced locus of Drosophila melanogaster. Genetics. 1991 Oct;129(2):423-41. PMID:1743486
↑ Joshi R, Passner JM, Rohs R, Jain R, Sosinsky A, Crickmore MA, Jacob V, Aggarwal AK, Honig B, Mann RS. Functional specificity of a Hox protein mediated by the recognition of minor groove structure. Cell. 2007 Nov 2;131(3):530-43. PMID:17981120 doi:10.1016/j.cell.2007.09.024

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2r5z"

@@ Line 1: / Line 1: @@
 ==Structure of Scr/Exd complex bound to a DNA sequence derived from the fkh gene==
 <StructureSection load='2r5z' size='340' side='right' caption='[[2r5z]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b8i|1b8i]], [[2r5y|2r5y]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Scr ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME]), exd ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</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=2r5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r5z OCA], [http://pdbe.org/2r5z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2r5z RCSB], [http://www.ebi.ac.uk/pdbsum/2r5z PDBsum]</span></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=2r5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r5z OCA], [http://pdbe.org/2r5z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2r5z RCSB], [http://www.ebi.ac.uk/pdbsum/2r5z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2r5z ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r5/2r5z_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r5/2r5z_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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=2r5z ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 31: / Line 32: @@
 ==See Also==
 *[[Group:USC-LCHS|USC-LCHS]]
-*[[Hox-DNA Recognition|Hox-DNA Recognition]]
+*[[Hox protein|Hox protein]]
 == References ==
 <references/>

2r5z

From Proteopedia

Revision as of 11:14, 5 September 2018

Structure of Scr/Exd complex bound to a DNA sequence derived from the fkh gene

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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