PMID- 10430869
OWN - NLM
STAT- MEDLINE
DCOM- 19990909
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 96
IP  - 16
DP  - 1999 Aug 3
TI  - Crystal structure of the alpha appendage of AP-2 reveals a recruitment platform
      for clathrin-coat assembly.
PG  - 8907-12
AB  - AP-2 adaptors regulate clathrin-bud formation at the cell surface by recruiting
      clathrin trimers to the plasma membrane and by selecting certain membrane
      proteins for inclusion within the developing clathrin-coat structure. These
      functions are performed by discrete subunits of the adaptor heterotetramer. The
      carboxyl-terminal appendage of the AP-2 alpha subunit appears to regulate the
      translocation of several endocytic accessory proteins to the bud site. We have
      determined the crystal structure of the alpha appendage at 1.4-A resolution by
      multiwavelength anomalous diffraction phasing. It is composed of two distinct
      structural modules, a beta-sandwich domain and a mixed alpha-beta platform
      domain. Structure-based mutagenesis shows that alterations to the molecular
      surface of a highly conserved region on the platform domain differentially affect
      associations of the appendage with amphiphysin, eps15, epsin, and AP180,
      revealing a common protein-binding interface.
FAU - Traub, L M
AU  - Traub LM
AD  - Department of Internal Medicine, Washington University School of Medicine, 660
      South Euclid Avenue, St. Louis, MO 63110, USA.
FAU - Downs, M A
AU  - Downs MA
FAU - Westrich, J L
AU  - Westrich JL
FAU - Fremont, D H
AU  - Fremont DH
LA  - eng
SI  - PDB/1QTP
SI  - PDB/1QTS
GR  - Wellcome Trust/United Kingdom
GR  - R01 DK053249/DK/NIDDK NIH HHS/United States
GR  - DK53249/DK/NIDDK 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  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Adaptor Proteins, Vesicular Transport)
RN  - 0 (Clathrin)
RN  - 0 (Macromolecular Substances)
RN  - 0 (Monomeric Clathrin Assembly Proteins)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Phosphoproteins)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (clathrin assembly protein AP180)
SB  - IM
CIN - Proc Natl Acad Sci U S A. 1999 Aug 3;96(16):8809-10. PMID: 10430846
MH  - Adaptor Proteins, Vesicular Transport
MH  - Amino Acid Sequence
MH  - Animals
MH  - Clathrin/chemistry/metabolism
MH  - Crystallography, X-Ray
MH  - Humans
MH  - Macromolecular Substances
MH  - Mice
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - *Monomeric Clathrin Assembly Proteins
MH  - Mutagenesis, Site-Directed
MH  - Nerve Tissue Proteins/*chemistry/metabolism
MH  - Phosphoproteins/*chemistry/metabolism
MH  - Protein Structure, Secondary
MH  - Recombinant Fusion Proteins/chemistry/metabolism
PMC - PMC17706
EDAT- 1999/08/04 00:00
MHDA- 1999/08/04 00:01
CRDT- 1999/08/04 00:00
PHST- 1999/08/04 00:00 [pubmed]
PHST- 1999/08/04 00:01 [medline]
PHST- 1999/08/04 00:00 [entrez]
AID - 10.1073/pnas.96.16.8907 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1999 Aug 3;96(16):8907-12. doi:
      10.1073/pnas.96.16.8907.