1bpo
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1bpo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bpo, resolution 2.6Å" /> '''CLATHRIN HEAVY-CHAIN...)
Next diff →
Revision as of 06:50, 18 November 2007
|
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 Sun Nov 18 08:57:45 2007
