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1c20
From Proteopedia
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| - | [[Image:1c20.gif|left|200px]] | + | [[Image:1c20.gif|left|200px]] |
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| - | '''SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN FROM THE DEAD RINGER PROTEIN''' | + | {{Structure |
| + | |PDB= 1c20 |SIZE=350|CAPTION= <scene name='initialview01'>1c20</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN FROM THE DEAD RINGER PROTEIN''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1C20 is a [ | + | 1C20 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=1C20 OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10545119 10545119] |
[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: dna-binding domain]] | [[Category: dna-binding domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:18:48 2008'' |
Revision as of 08:18, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN FROM THE DEAD RINGER PROTEIN
Overview
The 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.
About this Structure
1C20 is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 10:18:48 2008
