PMID- 10394364
OWN - NLM
STAT- MEDLINE
DCOM- 19990716
LR  - 20071114
IS  - 1097-2765 (Print)
IS  - 1097-2765 (Linking)
VI  - 3
IP  - 6
DP  - 1999 Jun
TI  - Functional organization of clathrin in coats: combining electron cryomicroscopy
      and X-ray crystallography.
PG  - 761-70
AB  - 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 A resolution by electron
      cryomicroscopy and of the clathrin terminal domain and linker at 2.6 A 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.
FAU - Musacchio, A
AU  - Musacchio A
AD  - Children's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA.
FAU - Smith, C J
AU  - Smith CJ
FAU - Roseman, A M
AU  - Roseman AM
FAU - Harrison, S C
AU  - Harrison SC
FAU - Kirchhausen, T
AU  - Kirchhausen T
FAU - Pearse, B M
AU  - Pearse BM
LA  - eng
GR  - GM36548/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Mol Cell
JT  - Molecular cell
JID - 9802571
RN  - 0 (Clathrin)
RN  - 114899-12-6 (Clathrin Heavy Chains)
SB  - IM
MH  - Clathrin/*chemistry/metabolism/ultrastructure
MH  - Clathrin Heavy Chains
MH  - Coated Pits, Cell-Membrane/chemistry/*ultrastructure
MH  - Coated Vesicles/chemistry/*ultrastructure
MH  - Cryoelectron Microscopy
MH  - Crystallization
MH  - Crystallography, X-Ray
MH  - Models, Molecular
MH  - Pliability
MH  - Protein Binding
MH  - Protein Conformation
EDAT- 1999/07/08 00:00
MHDA- 1999/07/08 00:01
CRDT- 1999/07/08 00:00
PHST- 1999/07/08 00:00 [pubmed]
PHST- 1999/07/08 00:01 [medline]
PHST- 1999/07/08 00:00 [entrez]
AID - S1097-2765(01)80008-3 [pii]
PST - ppublish
SO  - Mol Cell. 1999 Jun;3(6):761-70.