2PG1

Structural analysis of a cytoplasmic dynein Light Chain-Intermediate Chain complex

Summary for 2PG1

• Entry DOI: 10.2210/pdb2pg1/pdb
• Descriptor: Dynein light chain 1, cytoplasmic, Dynein light chain Tctex-type, Cytoplasmic dynein 1 intermediate chain 2, ... (5 entities in total)
• Functional Keywords: dynein intermediate chain, dynein light chain, lc8, pin, tctex1, structural protein
• Biological source: Drosophila melanogaster (fruit fly); More
• Cellular location: Cytoplasm, cytoskeleton: Q24117 Q62871; Cytoplasm, cytoskeleton (Probable): Q94524
• Total number of polymer chains: 12
• Total formula weight: 108256.85

Authors

Williams, J.C.,Hendrickson, W.A. (deposition date: 2007-04-06, release date: 2007-06-05, Last modification date: 2024-10-16)

Primary citation

Williams, J.C.,Roulhac, P.L.,Roy, A.G.,Vallee, R.B.,Fitzgerald, M.C.,Hendrickson, W.A.
Structural and thermodynamic characterization of a cytoplasmic dynein light chain-intermediate chain complex
Proc.Natl.Acad.Sci.Usa, 104:10028-10033, 2007

PubMed Abstract: 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.

PubMed: 17551010
DOI: 10.1073/pnas.0703614104

Experimental method

X-RAY DIFFRACTION (2.8 Å)