2pg1
From Proteopedia
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[[Image:2pg1.jpg|left|200px]] | [[Image:2pg1.jpg|left|200px]] | ||
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'''Structural analysis of a cytoplasmic dynein Light Chain-Intermediate Chain complex''' | '''Structural analysis of a cytoplasmic dynein Light Chain-Intermediate Chain complex''' | ||
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[[Category: Hendrickson, W A.]] | [[Category: Hendrickson, W A.]] | ||
[[Category: Williams, J C.]] | [[Category: Williams, J C.]] | ||
| - | [[Category: | + | [[Category: Dynein intermediate chain]] |
| - | [[Category: | + | [[Category: Dynein light chain]] |
| - | [[Category: | + | [[Category: Lc8]] |
| - | [[Category: | + | [[Category: Pin]] |
| - | [[Category: | + | [[Category: Tctex1]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 13:02:29 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 10:02, 4 May 2008
Structural analysis of a cytoplasmic dynein Light Chain-Intermediate Chain complex
Overview
Cytoplasmic dynein is a microtubule-based motor protein complex that plays important roles in a wide range of fundamental cellular processes, including vesicular transport, mitosis, and cell migration. A single major form of cytoplasmic dynein associates with membranous organelles, mitotic kinetochores, the mitotic and migratory cell cortex, centrosomes, and mRNA complexes. The ability of cytoplasmic dynein to recognize such diverse forms of cargo is thought to be associated with its several accessory subunits, which reside at the base of the molecule. The dynein light chains (LCs) LC8 and TcTex1 form a subcomplex with dynein intermediate chains, and they also interact with numerous protein and ribonucleoprotein partners. This observation has led to the hypothesis that these subunits serve to tether cargo to the dynein motor. Here, we present the structure and a thermodynamic analysis of a complex of LC8 and TcTex1 associated with their intermediate chain scaffold. The intermediate chains effectively block the major putative cargo binding sites within the light chains. These data suggest that, in the dynein complex, the LCs do not bind cargo, in apparent disagreement with a role for LCs in dynein cargo binding interactions.
About this Structure
2PG1 is a Protein complex structure of sequences from Drosophila melanogaster and Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structural and thermodynamic characterization of a cytoplasmic dynein light chain-intermediate chain complex., Williams JC, Roulhac PL, Roy AG, Vallee RB, Fitzgerald MC, Hendrickson WA, Proc Natl Acad Sci U S A. 2007 Jun 12;104(24):10028-33. Epub 2007 Jun 5. PMID:17551010 Page seeded by OCA on Sun May 4 13:02:29 2008
