2pg1
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Structural analysis of a cytoplasmic dynein Light Chain-Intermediate Chain complex
OverviewOverview
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 StructureAbout this Structure
2PG1 is a Protein complex structure of sequences from Drosophila melanogaster and Rattus norvegicus with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
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
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