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Abstract:
The sorting of specific proteins into clathrin-coated pits and the
mechanics of membrane invagination are determined by assembly of the
clathrin lattice. Recent structures of a six-fold barrel clathrin coat
at 21 Angstrom resolution by electron cryomicroscopy and of the clathrin
terminal domain and linker at 2.6 Angstrom by X-ray crystallography
together show how domains of clathrin interact and orient within the
coat and reveal the strongly puckered shape and conformational
variability of individual triskelions. The beta propeller of the
terminal domain faces the membrane so that recognition segments from
adaptor proteins can extend along its lateral grooves. Clathrin legs
adapt to different coat environments in the barrel by flexing along a
segment at the knee that is free of contacts with other molecules.
