Functional organization of clathrin in coats: Combining electron cryomicroscopy and x-ray crystallography

被引：96

作者：

Musacchio, A

Smith, CJ

Roseman, AM

Harrison, SC

Kirchhausen, T ^{[1
]}

Pearse, BMF

机构：

[1] Harvard Univ, Sch Med, Dept Cell Biol, Boston, MA 02115 USA

[2] Harvard Univ, Sch Med, Ctr Blood Res, Boston, MA 02115 USA

[3] Harvard Univ, Sch Med, Childrens Hosp, Boston, MA 02115 USA

[4] Harvard Univ, Sch Med, Howard Hughes Med Inst, Mol Med Lab, Boston, MA 02115 USA

[5] MRC, Mol Biol Lab, Cambridge CB2 2QH, England

来源：

MOLECULAR CELL | 1999年 / 3卷 / 06期

关键词：

D O I：

10.1016/S1097-2765(01)80008-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The sorting of specific proteins into clathrin-coated pits and the mechanics of membrane invagination are determined by assembly of the clathrin lattice. Recent structures of a six-fold barrel clathrin coat at 21 Angstrom resolution by electron cryomicroscopy and of the clathrin terminal domain and linker at 2.6 Angstrom by X-ray crystallography together show how domains of clathrin interact and orient within the coat and reveal the strongly puckered shape and conformational variability of individual triskelions. The beta propeller of the terminal domain faces the membrane so that recognition segments from adaptor proteins can extend along its lateral grooves. Clathrin legs adapt to different coat environments in the barrel by flexing along a segment at the knee that is free of contacts with other molecules.

引用

页码：761 / 770

页数：10

共 51 条

[21] CLATHRIN HEAVY-CHAIN - MOLECULAR-CLONING AND COMPLETE PRIMARY STRUCTURE [J].