This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1c20

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1c20.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1c20.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1c20| PDB=1c20 | SCENE= }}
{{STRUCTURE_1c20| PDB=1c20 | SCENE= }}
-
'''SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN FROM THE DEAD RINGER PROTEIN'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10545119}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10545119 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10545119}}
==About this Structure==
==About this Structure==
-
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].
+
1C20 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C20 OCA].
==Reference==
==Reference==
Line 27: Line 31:
[[Category: At-rich interaction domain]]
[[Category: At-rich interaction domain]]
[[Category: Dna-binding domain]]
[[Category: Dna-binding domain]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:14:16 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:05:58 2008''

Revision as of 17:06, 30 June 2008

Image:1c20.png

Template:STRUCTURE 1c20

SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN FROM THE DEAD RINGER PROTEIN

Template:ABSTRACT PUBMED 10545119

About this Structure

1C20 is a Single protein structure of sequence from Drosophila melanogaster. Full experimental 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 Mon Jun 30 20:05:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1c20"
Personal tools