Figure 1.
FIG. 1. Molecular structure of intact cytoplasmic dynein.
The cytoplasmic dynein motor is a dimer containing two identical
heavy chain subunits of molecular mass 520 kDa. The core of the
motor, formed by the C-terminal two-thirds of the heavy chain,
comprises a ring of six AAA ATPase domains, depicted here in
blue and purple. The MTBD (blue) protrudes from the AAA core on
a coiled-coil stalk (gray). The attachment of cargo to the
dynein motor involves light and intermediate chain subunits
(green) that are associated with the N-terminal third of the
heavy chain. This figure was adapted from Ref. 2 with permission.
The above figure is reprinted
from an Open Access publication published by the ASBMB:
J Biol Chem
(2005,
280,
23960-23965)
copyright 2005.
520 kDa. The core of the
motor, formed by the C-terminal two-thirds of the heavy chain,
comprises a ring of six AAA ATPase domains, depicted here in
blue and purple. The MTBD (blue) protrudes from the AAA core on
a coiled-coil stalk (gray). The attachment of cargo to the
dynein motor involves light and intermediate chain subunits
(green) that are associated with the N-terminal third of the
heavy chain. This figure was adapted from Ref. 2 with permission.