Structural highlights
Function
CLH1_RAT Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ ter Haar E, Musacchio A, Harrison SC, Kirchhausen T. Atomic structure of clathrin: a beta propeller terminal domain joins an alpha zigzag linker. Cell. 1998 Nov 13;95(4):563-73. PMID:9827808
