Polycystic kidney disease: the complete structure of the PKD1 gene and its protein

Article Abstract:

The 14.5 kb PKD1 transcript obtained from a sequence of 46 exons encodes for a 4304 amino acid polypeptide with an unusual domain architecture. The amino terminal of this protein has five protein domains which include two leucine-rich repeats surrounded by cystine-rich domains, an LDL-A domain, a C-type lectin domain and a novel 80 amino acid sequence, suggesting that this protein can bind either to more than one molecule or to multiple sites of a molecule in the extracellular domain. The protein may be involved in adhesive protein-protein and protein-carbohydrate interactions in the extracellular matrix.

Research, Genetic aspects, Polycystic kidney disease, Protein binding, Protein research, Extracellular matrix

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Single-molecule analysis of dynein processivity and stepping behavior

Article Abstract:

Structural and single-molecule analysis is used to show that processivity requires two dynein motor domains but does not require dynein's tail domain or any associated subunits. The variable step size and direction of the two motor domains suggest a considerable diffusion component to its size, which differs from Kinesin-1 but is similar to myosin VI.

Dynein, Myosin

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