2a24: Difference between revisions

Revision as of 15:43, 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:2a24.png

Template:STRUCTURE 2a24

HADDOCK Structure of HIF-2a/ARNT PAS-B HeterodimerHADDOCK Structure of HIF-2a/ARNT PAS-B Heterodimer

Template:ABSTRACT PUBMED 16181639

About this StructureAbout this Structure

2A24 is a Protein complex structure of sequences from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

Structural basis of ARNT PAS-B dimerization: use of a common beta-sheet interface for hetero- and homodimerization., Card PB, Erbel PJ, Gardner KH, J Mol Biol. 2005 Oct 28;353(3):664-77. Epub 2005 Sep 6. PMID:16181639

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

OCA

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-[[Image:2a24.gif|left|200px]]
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-'''HADDOCK Structure of HIF-2a/ARNT PAS-B Heterodimer'''
+===HADDOCK Structure of HIF-2a/ARNT PAS-B Heterodimer===
-==Overview==
+<!--
-The aryl hydrocarbon receptor nuclear translocator (ARNT) is a promiscuous bHLH-PAS (Per-ARNT-Sim) protein that forms heterodimeric transcriptional regulator complexes with several other bHLH-PAS subunits to control a variety of biological pathways, some of which are centrally involved in disease initiation and/or progression. One of these is the hypoxia response pathway, which allows eukaryotic cells to respond to low oxygen tension via the formation of a heterodimeric complex between ARNT and another bHLH-PAS protein, the hypoxia-inducible factor alpha (HIF-alpha). We have previously shown that the C-terminal PAS domains of an HIF-alpha isoform (HIF-2alpha) and ARNT interact in vitro, and that mutations in the solvent-exposed beta-sheet surface of the HIF-2alpha domain not only disrupt this interaction, but also greatly attenuate the hypoxia response in living cells. Here, we have solved the solution structure of the corresponding PAS domain of ARNT and show that it utilizes a very similar interface for the interaction with the HIF-2alpha PAS domain. We also show that this domain self-associates in a concentration-dependent manner, and that the interface used in this homodimeric complex is very similar to that used in the formation of heterodimer. In addition, using experimentally derived NMR restraints, we used the program HADDOCK to calculate a low-resolution model of the complex formed in solution by these two PAS domains, and confirm the validity of this model using site-directed spin labeling to obtain long-range distance information in solution. With this information, we propose a model for the mode of multi-PAS domain interaction in bHLH-PAS transcriptional activation complexes.
+The line below this paragraph, {{ABSTRACT_PUBMED_16181639}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16181639 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16181639}}
 ==About this Structure==
-A24 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A24 OCA].
+A24 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A24 OCA].
 ==Reference==
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