作者: Andrea Musacchio , Corinne J Smith , Alan M Roseman , Stephen C Harrison , Tomas Kirchhausen
DOI: 10.1016/S1097-2765(01)80008-3
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摘要: Abstract The sorting of specific proteins into clathrin-coated pits and the mechanics membrane invagination are determined by assembly clathrin lattice. Recent structures a six-fold barrel coat at 21 A resolution electron cryomicroscopy terminal domain linker 2.6 X-ray crystallography together show how domains interact orient within reveal strongly puckered shape conformational variability individual triskelions. β propeller faces so that recognition segments from adaptor can extend along its lateral grooves. Clathrin legs adapt to different environments in flexing segment knee is free contacts with other molecules.