1bpo | pdb_00001bpo
CLATHRIN HEAVY-CHAIN TERMINAL DOMAIN AND LINKER
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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
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