2KIA: Solution structure of Myosin VI C-terminal cargo-binding domain

Myosin VI is the only known molecular motor that moves toward the minus ends of actin filaments; thus, it plays unique roles in diverse cellular processes. The processive walking of myosin VI on actin filaments requires dimerization of the motor, but the protein can also function as a nonprocessive monomer. The molecular mechanism governing the monomer-dimer conversion is not clear. We report the high-resolution NMR structure of the cargo-free myosin VI cargo-binding domain (CBD) and show that it is a stable monomer in solution. The myosin VI CBD binds to a fragment of the clathrin-coated vesicle adaptor Dab2 with a high affinity, and the X-ray structure of the myosin VI CBD in complex with Dab2 reveals that the motor undergoes a cargo-binding-mediated dimerization. The cargo-binding-induced dimerization may represent a general paradigm for the regulation of processivity for myosin VI as well as other myosins, including myosin VII and myosin X.
PDB ID: 2KIADownload
MMDB ID: 76961
PDB Deposition Date: 2009/4/29
Updated in MMDB: 2009/09
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Molecular Components in 2KIA
Label Count Molecule
Protein (1 molecule)
Myosin-vi(Gene symbol: Myo6)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB