1c20: Difference between revisions
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<StructureSection load='1c20' size='340' side='right'caption='[[1c20]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''> | <StructureSection load='1c20' size='340' side='right'caption='[[1c20]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1c20]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C20 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C20 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1c20]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C20 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C20 FirstGlance]. <br> | ||
</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=1c20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c20 OCA], [https://pdbe.org/1c20 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c20 RCSB], [https://www.ebi.ac.uk/pdbsum/1c20 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c20 ProSAT]</span></td></tr> | </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=1c20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c20 OCA], [https://pdbe.org/1c20 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c20 RCSB], [https://www.ebi.ac.uk/pdbsum/1c20 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c20 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Drome]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Clubb, R T]] | [[Category: Clubb, R T]] | ||
Revision as of 13:31, 16 February 2022
SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN FROM THE DEAD RINGER PROTEINSOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN FROM THE DEAD RINGER PROTEIN
Structural highlights
Function[DRI_DROME] Transcription factor which is a downstream target of gcm and repo. Directly or indirectly activates the transcription of locos and pros, which are essential for the development of some glial cells. Plays an essential role in defining the cell shape and migration characteristics of longitudinal glia that enable them to establish a normal axon scaffold.[1] [2] 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 PubMedThe Dead ringer protein from Drosophila melanogaster is a transcriptional regulatory protein required for early embryonic development. It is the founding member of a large family of DNA binding proteins that interact with DNA through a highly conserved domain called the AT-rich interaction domain (ARID). The solution structure of the Dead ringer ARID (residues Gly262-Gly398) was determined using NMR spectroscopy. The ARID forms a unique globular structure consisting of eight alpha-helices and a short two-stranded anti-parallel beta-sheet. Amino acid sequence homology indicates that ARID DNA binding proteins are partitioned into three structural classes: (i) minimal ARID proteins that consist of a core domain formed by six alpha-helices; (ii) ARID proteins that supplement the core domain with an N-terminal alpha-helix; and (iii) extended-ARID proteins, which contain the core domain and additional alpha-helices at their N- and C-termini. Studies of the Dead ringer-DNA complex suggest that the major groove of DNA is recognized by a helix-turn-helix (HTH) motif and the adjacent minor grooves are contacted by a beta-hairpin and C-terminal alpha-helix. Primary homology suggests that all ARID-containing proteins contact DNA through the HTH and hairpin structures, but only extended-ARID proteins supplement this binding surface with a terminal helix. Solution structure of the DNA binding domain from Dead ringer, a sequence-specific AT-rich interaction domain (ARID).,Iwahara J, Clubb RT EMBO J. 1999 Nov 1;18(21):6084-94. PMID:10545119[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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