English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Atomic Structure of Clathrin: A β Propeller Terminal Domain Joins an α Zigzag Linker

ter Haar, E., Musacchio, A., Harrison, S. C., & Kirchhausen, T. (1998). Atomic Structure of Clathrin: A β Propeller Terminal Domain Joins an α Zigzag Linker. CELL, 95(4), 563-573. doi:10.1016/S0092-8674(00)81623-2.

Item is

Files

show Files

Locators

show

Creators

show
hide
 Creators:
ter Haar, Ernst1, Author
Musacchio, Andrea2, Author           
Harrison, Stephen C.3, Author
Kirchhausen, Tomas1, Author
Affiliations:
1Department of Cell Biology and Center for Blood Research, Harvard Medical School, Boston, Massachusetts 02115-5701, USA, ou_persistent22              
2Abt. I:Mechanistische Zellbiologie, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753287              
3Howard Hughes Medical Institute, Boston, Massachusetts 02115, USA, ou_persistent22              

Content

show
hide
Free keywords: -
 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 Angstrom 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.

Details

show
hide
Language(s):
 Dates: 1998
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: CELL
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 95 (4) Sequence Number: - Start / End Page: 563 - 573 Identifier: ISSN: 0092-8674