1re6: Difference between revisions

Revision as of 18:29, 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:1re6.png

Template:STRUCTURE 1re6

Localisation of Dynein Light Chains 1 and 2 and their Pro-apoptotic LigandsLocalisation of Dynein Light Chains 1 and 2 and their Pro-apoptotic Ligands

Template:ABSTRACT PUBMED 14561217

About this StructureAbout this Structure

1RE6 is a Single protein structure of sequence from Mus musculus. Full experimental information is available from OCA.

ReferenceReference

Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands., Day CL, Puthalakath H, Skea G, Strasser A, Barsukov I, Lian LY, Huang DC, Hinds MG, Biochem J. 2004 Feb 1;377(Pt 3):597-605. PMID:14561217

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-'''Localisation of Dynein Light Chains 1 and 2 and their Pro-apoptotic Ligands'''
+===Localisation of Dynein Light Chains 1 and 2 and their Pro-apoptotic Ligands===
-==Overview==
+<!--
-The dynein and myosin V motor complexes are multi-protein structures that function to transport molecules and organelles within the cell. DLC (dynein light-chain) proteins, found as components of both dynein and myosin V motor complexes, connect the complexes to their cargoes. One of the roles of these motor complexes is to selectively sequester the pro-apoptotic 'BH3-only' (Bcl-2 homology 3-only) proteins, Bim (Bcl-2-interacting mediator of cell death) and Bmf (Bcl-2-modifying factor), and so regulate their cell death-inducing function. In vivo DLC2 is found exclusively as a component of the myosin V motor complex and Bmf binds DLC2 selectively. On the other hand, Bim interacts with DLC1 (LC8), an integral component of the dynein motor complex. The two DLCs share 93% sequence identity yet show unambiguous in vivo specificity for their respective BH3-only ligands. To investigate this specificity the three-dimensional solution structure of DLC2 was elucidated using NMR spectroscopy. In vitro structural and mutagenesis studies show that Bmf and Bim have identical binding characteristics to recombinant DLC2 or DLC1. Thus the selectivity shown by Bmf and Bim for binding DLC1 or DLC2, respectively, does not reside in their DLC-binding domains. Remarkably, mutational analysis of DLC1 and DLC2 indicates that a single surface residue (residue 41) determines the specific localization of DLCs with their respective motor complexes. These results suggest a molecular mechanism for the specific compartmentalization of DLCs and their pro-apoptotic cargoes and implicate other protein(s) in defining the specificity between the cargoes and the DLC proteins.
+The line below this paragraph, {{ABSTRACT_PUBMED_14561217}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14561217 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_14561217}}
 ==About this Structure==
-RE6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RE6 OCA].
+RE6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RE6 OCA].
 ==Reference==
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 [[Category: Dimer]]
 [[Category: Dynein light chain]]
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