2han: Difference between revisions

Revision as of 23:08, 27 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:2han.png

Template:STRUCTURE 2han

Structural basis of heterodimeric ecdysteroid receptor interaction with natural response element hsp27 gene promoterStructural basis of heterodimeric ecdysteroid receptor interaction with natural response element hsp27 gene promoter

Template:ABSTRACT PUBMED 17426125

About this StructureAbout this Structure

2HAN is a Protein complex structure of sequences from Drosophila melanogaster. Full crystallographic information is available from OCA.

ReferenceReference

Novel DNA-binding element within the C-terminal extension of the nuclear receptor DNA-binding domain., Jakob M, Kolodziejczyk R, Orlowski M, Krzywda S, Kowalska A, Dutko-Gwozdz J, Gwozdz T, Kochman M, Jaskolski M, Ozyhar A, Nucleic Acids Res. 2007;35(8):2705-18. Epub 2007 Apr 10. PMID:17426125

Page seeded by OCA on Sun Jul 27 23:08:08 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:2han.gif|left|200px]]
+{{Seed}}
+[[Image:2han.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2han|  PDB=2han  |  SCENE=  }}
-'''Structural basis of heterodimeric ecdysteroid receptor interaction with natural response element hsp27 gene promoter'''
+===Structural basis of heterodimeric ecdysteroid receptor interaction with natural response element hsp27 gene promoter===
-==Overview==
+<!--
-The heterodimer of the ecdysone receptor (EcR) and ultraspiracle (Usp), members of the nuclear receptors superfamily, is considered as the functional receptor for ecdysteroids initiating molting and metamorphosis in insects. Here we report the 1.95 A structure of the complex formed by the DNA-binding domains (DBDs) the EcR and the Usp, bound to the natural pseudopalindromic response element. Comparison of the structure with that obtained previously, using an idealized response element, shows how the EcRDBD, which has been previously reported to possess extraordinary flexibility, accommodates DNA-induced structural changes. Part of the C-terminal extension (CTE) of the EcRDBD folds into an alpha-helix whose location in the minor groove does not match any of the locations previously observed for nuclear receptors. Mutational analyses suggest that the alpha-helix is a component of EcR-box, a novel element indispensable for DNA-binding and located within the nuclear receptor CTE. This element seems to be a general feature of all known EcRs.
+The line below this paragraph, {{ABSTRACT_PUBMED_17426125}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17426125 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17426125}}
 ==About this Structure==
@@ Line 38: / Line 42: @@
 [[Category: Transcription regulation]]
 [[Category: Zinc finger]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 06:03:45 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:08:08 2008''