1wid: Difference between revisions

Revision as of 03:18, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1wid.png

Template:STRUCTURE 1wid

Solution Structure of the B3 DNA-Binding Domain of RAV1Solution Structure of the B3 DNA-Binding Domain of RAV1

Template:ABSTRACT PUBMED 15548737

About this StructureAbout this Structure

1WID is a Single protein structure of sequence from Arabidopsis thaliana. Full experimental information is available from OCA.

ReferenceReference

Solution structure of the B3 DNA binding domain of the Arabidopsis cold-responsive transcription factor RAV1., Yamasaki K, Kigawa T, Inoue M, Tateno M, Yamasaki T, Yabuki T, Aoki M, Seki E, Matsuda T, Tomo Y, Hayami N, Terada T, Shirouzu M, Osanai T, Tanaka A, Seki M, Shinozaki K, Yokoyama S, Plant Cell. 2004 Dec;16(12):3448-59. Epub 2004 Nov 17. PMID:15548737

Page seeded by OCA on Mon Jul 28 03:18:04 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1wid.jpg|left|200px]]
+{{Seed}}
+[[Image:1wid.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1wid|  PDB=1wid  |  SCENE=  }}
-'''Solution Structure of the B3 DNA-Binding Domain of RAV1'''
+===Solution Structure of the B3 DNA-Binding Domain of RAV1===
-==Overview==
+<!--
-The B3 DNA binding domain is shared amongst various plant-specific transcription factors, including factors involved in auxin-regulated and abscisic acid-regulated transcription. Herein, we report the NMR solution structure of the B3 domain of the Arabidopsis thaliana cold-responsive transcription factor RAV1. The structure consists of a seven-stranded open beta-barrel and two alpha-helices located at the ends of the barrel and is significantly similar to the structure of the noncatalytic DNA binding domain of the restriction enzyme EcoRII. An NMR titration experiment revealed a DNA recognition interface that enabled us to propose a structural model of the protein-DNA complex. The locations of the DNA-contacting residues are also likely to be similar to those of the EcoRII DNA binding domain.
+The line below this paragraph, {{ABSTRACT_PUBMED_15548737}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15548737 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15548737}}
 ==About this Structure==
-WID is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WID OCA].
+WID is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WID OCA].
 ==Reference==
@@ Line 31: / Line 35: @@
 [[Category: Rsgi]]
 [[Category: Structural genomic]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 13:43:07 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:18:04 2008''