1bpo
From Proteopedia
CLATHRIN HEAVY-CHAIN TERMINAL DOMAIN AND LINKER
Overview
Clathrin triskelions form the lattice that organizes recruitment of proteins to coated pits and helps drive vesiculation of the lipid bilayer. We report the crystal structure at 2.6 A resolution of a 55 kDa N-terminal fragment from the 190 kDa clathrin heavy chain. The structure comprises the globular "terminal domain" and the linker that joins it to the end of a triskelion leg. The terminal domain is a seven-blade beta propeller, a structure well adapted to interaction with multiple partners, such as the AP-1 and AP-2 sorting adaptor complexes and the nonvisual arrestins. The linker is an alpha-helical zigzag emanating from the propeller domain. We propose that this simple motif may extend into the rest of the clathrin leg.
About this Structure
1BPO is a Single protein structure of sequence from Rattus norvegicus. The following page contains interesting information on the relation of 1BPO with [Clathrin]. Full crystallographic information is available from OCA.
Reference
Atomic structure of clathrin: a beta propeller terminal domain joins an alpha zigzag linker., ter Haar E, Musacchio A, Harrison SC, Kirchhausen T, Cell. 1998 Nov 13;95(4):563-73. PMID:9827808 Page seeded by OCA on Fri May 2 11:48:18 2008
