PMID- 10380931
OWN - NLM
STAT- MEDLINE
DCOM- 19990722
LR  - 20190705
IS  - 0092-8674 (Print)
IS  - 0092-8674 (Linking)
VI  - 97
IP  - 6
DP  - 1999 Jun 11
TI  - A structural explanation for the binding of multiple ligands by the alpha-adaptin
      appendage domain.
PG  - 805-15
AB  - The alpha subunit of the endocytotic AP2 adaptor complex contains a 30 kDa
      "appendage" domain, which is joined to the rest of the protein via a flexible
      linker. The 1.9 A resolution crystal structure of this domain reveals a single
      binding site for its ligands, which include amphiphysin, Eps15, and epsin. This
      domain when overexpressed in COS7 fibroblasts is shown to inhibit transferrin
      uptake, whereas mutants in which interactions with its binding partners are
      abolished do not. DPF/W motifs present in appendage domain-binding partners are
      shown to play a crucial role in their interactions with the domain. A single site
      for binding multiple ligands would allow for temporal and spatial regulation in
      the recruitment of components of the endocytic machinery.
FAU - Owen, D J
AU  - Owen DJ
AD  - MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
FAU - Vallis, Y
AU  - Vallis Y
FAU - Noble, M E
AU  - Noble ME
FAU - Hunter, J B
AU  - Hunter JB
FAU - Dafforn, T R
AU  - Dafforn TR
FAU - Evans, P R
AU  - Evans PR
FAU - McMahon, H T
AU  - McMahon HT
LA  - eng
SI  - PDB/1B9K
PT  - Journal Article
PL  - United States
TA  - Cell
JT  - Cell
JID - 0413066
RN  - 0 (Adaptor Protein Complex 2)
RN  - 0 (Adaptor Protein Complex alpha Subunits)
RN  - 0 (Adaptor Proteins, Vesicular Transport)
RN  - 0 (Ligands)
RN  - 0 (Membrane Proteins)
SB  - IM
MH  - Adaptor Protein Complex 2
MH  - Adaptor Protein Complex alpha Subunits
MH  - Adaptor Proteins, Vesicular Transport
MH  - Amino Acid Sequence
MH  - Animals
MH  - Binding Sites
MH  - COS Cells
MH  - Crystallography, X-Ray
MH  - Endocytosis
MH  - Ligands
MH  - Membrane Proteins/*chemistry/genetics/metabolism
MH  - Molecular Sequence Data
MH  - Protein Conformation
EDAT- 1999/06/25 00:00
MHDA- 1999/06/25 00:01
CRDT- 1999/06/25 00:00
PHST- 1999/06/25 00:00 [pubmed]
PHST- 1999/06/25 00:01 [medline]
PHST- 1999/06/25 00:00 [entrez]
AID - S0092-8674(00)80791-6 [pii]
AID - 10.1016/s0092-8674(00)80791-6 [doi]
PST - ppublish
SO  - Cell. 1999 Jun 11;97(6):805-15. doi: 10.1016/s0092-8674(00)80791-6.