1re6: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1re6.jpg|left|200px]] | [[Image:1re6.jpg|left|200px]] | ||
'''Localisation of Dynein Light Chains 1 and 2 and their Pro-apoptotic Ligands''' | {{Structure | ||
|PDB= 1re6 |SIZE=350|CAPTION= <scene name='initialview01'>1re6</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= DLC2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |||
}} | |||
'''Localisation of Dynein Light Chains 1 and 2 and their Pro-apoptotic Ligands''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1RE6 is a [ | 1RE6 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]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14561217 14561217] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 25: | Line 34: | ||
[[Category: dynein light chain]] | [[Category: dynein light chain]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:50:24 2008'' | ||
Revision as of 14:50, 20 March 2008
| |||||||
| Gene: | DLC2 (Mus musculus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Localisation of Dynein Light Chains 1 and 2 and their Pro-apoptotic Ligands
OverviewOverview
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.
About this StructureAbout this Structure
1RE6 is a Single protein structure of sequence from Mus musculus. Full crystallographic 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
Page seeded by OCA on Thu Mar 20 13:50:24 2008