1BPO
CLATHRIN HEAVY-CHAIN TERMINAL DOMAIN AND LINKER
Summary for 1BPO
| Entry DOI | 10.2210/pdb1bpo/pdb |
| Descriptor | PROTEIN (CLATHRIN) (2 entities in total) |
| Functional Keywords | clathrin endocytosis beta-propeller coated-pits, membrane protein |
| Biological source | Rattus norvegicus (Norway rat) |
| Total number of polymer chains | 3 |
| Total formula weight | 165270.50 |
| Authors | Harr, E.T.,Musacchio, A.,Harrison, S.C.,Kirchhausen, T. (deposition date: 1998-08-11, release date: 1998-12-16, Last modification date: 2023-12-27) |
| Primary citation | Haar, E.T.,Musacchio, A.,Harrison, S.C.,Kirchhausen, T. Atomic structure of clathrin: a beta propeller terminal domain joins an alpha zigzag linker. Cell(Cambridge,Mass.), 95:563-573, 1998 Cited by PubMed Abstract: 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. PubMed: 9827808DOI: 10.1016/S0092-8674(00)81623-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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